Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.

Based on these considerations, we set out the program with the peptide HIV-1 fusion inhibitor C34, a 34-amino-acid peptide from the C-terminal heptad repeat region of HIV-1 gp41 envelope protein. At its C terminus, C34 shares an identical 24-amino-acid sequence with the N terminus of enfuvirtide. Nevertheless, these two peptides are believed to utilize nonoverlapping molecular targets in the HIV-1 membrane glycoprotein gp41. Assisted by the crystal structure of C34 in complex with HIV-1 gp41 N peptides, three residues of C34 not involved in target binding were replaced by lysine and glutamic acid to improve the solubility and antiviral activity. This peptide, FB006, is to be chemically modified further and conjugated to albumin. Albumins of rodents, rabbits, dogs, monkeys, and humans all possess a conserved cysteine residue (Cys34 in humans) that has the only free thiol group in the protein. To enable binding to this thiol group, FB006 was modified by 3-maleimidopropionic acid (MPA), which allows an irreversible reaction between the maleimide and the free thiol to form a specific 1:1 peptide-albumin conjugate. Guided by the crystal structure of the HIV-1 gp41 ectodomain, we chemically modified FB006 with a single MPA at different residual positions. These peptides were conjugated to human serum albumin (HSA) in vitro and subjected to a human peripheral blood mononuclear cell (PBMC) assay to determine their anti-HIV activities. Based on the results, a lead molecule named FB006M was selected for further studies.