Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.

Based on this observation we were very much projected towards the conjugation of elastin based peptides with varying chain length and hydrophobicity. We focused our attention on tetrapeptide elastin sequences with varying hydrophobicity. Among the analogs tested GGAP (29), GGIP (30) and GGFP (31), the latter has exhibited more activity i.e., GGFP with Phe unit has exerted nearly two times more potent activity than the antibiotics used where as the other two tetrapeptides conjugated heterocycle have shown comparatively less activity than GGFP which could be due to less hydrophobicity of amino acids present at the second position. Thus the order of activity among tetrapeptide conjugates is GGFP > GGIP > GGAP. In the light of the above findings, our subsequent goal was to incorporate GVGVP and GFGFP pentapeptide elastin sequences for conjugation. The pentapeptide conjugates have shown more than two fold potent activity compared to reference drugs used. Among these, GFGFP conjugate (33) has shown slight enhancement in the activity over GVGVP conjugate (32) which may be due to the presence of two more hydrophobic Phe units in 33. Inspection of the results further revealed that the conjugate 26 having single Phe residue has shown enhanced activity. On the other hand, retaining of only one Phe unit and increasing the peptide chain length has caused further increase in the activity (~two times) which is evident from the conjugate GGFP (31). Similarly, the remaining two tetrapeptide conjugates GGIP and GGAP have shown increased activity compared to Phe alone (26). Also, when the length of the peptide chain increased as well as two Phe residues were introduced (greater hydrophobicity) as in GFGFP (33) has exhibited two times greater activity than the standard drugs. This trend was followed in GVGVP conjugate (32) also. Hence, it can be inferred that as the length of the peptide chain as well as the hydrophobicity increases the activity also increases. Thus, the order of activity of the heterocyclic conjugated peptides is found to be GFGFP > GVGVP > GGFP > GGIP > GGAP > Phe > Trp > Tyr.