Peptide_ID	Peptide_Name	efficacy_type	efficacy_value_d	Binding Affinity Assay	Experimental Condition	REF_ID
PEP00174	BT1718 Bicycle peptide	K<sub>D</sub>	3 nM	.	.	REF003371
PEP00105	Ga-DOTA-TATEa octreotide	IC50	377 &plusmn; 18 nmol/L	"CHO-K1 and CCL39 cells stably expressing human sst1-5 (hsst1-5) were grown as described previously . All culture reagents were supplied by GIBCO/BRL and Life Technologies (Grand Island, NY). Cell membrane pellets were prepared and receptor autoradiography was performed on pellet sections (mounted on microscope slides), as described in detail previously . For each of the tested compounds, complete displacement experiments were performed with the universal somatostatin radioligand [125I]-[Leu8,D-Trp22,Trp25]-somatostatin-28 using increasing concentrations of the MetalloIII-DOTA-peptide ranging from 0.1 to 1,000nmol/l. Somatostatin-28 was run in parallel as control using the same increasing concentrations. IC50values were calculated after quantification of the data using a computer-assisted image processing system. Tissue standards (autoradiographic [125I] microscales, Amersham, UK) containing known amounts of isotopes, cross-calibrated to tissue-equivalent ligand concentrations, were used for quantification . The concentrations of the peptide solutions were measured by UV spectroscopy (NOC-ATE, 280nm = 9,855cm-1mol-1dm3, BOC-ATE, 280nm = 7,570cm-1mol-1dm3, TOC, 280nm> = 6,849cm-1mol-1dm3, NOC,280nm> = 9,850cm-1mol-1dm3)."	CHO-K1 and CCL39 cellsSSRT5	REF00165; REF003281
PEP00105	Y-DOTA-TATEa octreotide	IC50	187 &plusmn; 50 nmol/L	"CHO-K1 and CCL39 cells stably expressing human sst1-5 (hsst1-5) were grown as described previously . All culture reagents were supplied by GIBCO/BRL and Life Technologies (Grand Island, NY). Cell membrane pellets were prepared and receptor autoradiography was performed on pellet sections (mounted on microscope slides), as described in detail previously . For each of the tested compounds, complete displacement experiments were performed with the universal somatostatin radioligand [125I]-[Leu8,D-Trp22,Trp25]-somatostatin-28 using increasing concentrations of the MetalloIII-DOTA-peptide ranging from 0.1 to 1,000nmol/l. Somatostatin-28 was run in parallel as control using the same increasing concentrations. IC50values were calculated after quantification of the data using a computer-assisted image processing system. Tissue standards (autoradiographic [125I] microscales, Amersham, UK) containing known amounts of isotopes, cross-calibrated to tissue-equivalent ligand concentrations, were used for quantification . The concentrations of the peptide solutions were measured by UV spectroscopy (NOC-ATE, 280nm = 9,855cm-1mol-1dm3, BOC-ATE, 280nm = 7,570cm-1mol-1dm3, TOC, 280nm> = 6,849cm-1mol-1dm3, NOC,280nm> = 9,850cm-1mol-1dm3)."	CHO-K1 and CCL39 cellsSSRT5	REF00165; REF003281
PEP00105	Y-DOTA-TATEa octreotide	IC50	523 &plusmn; 239 nmol/L	"CHO-K1 and CCL39 cells stably expressing human sst1-5 (hsst1-5) were grown as described previously . All culture reagents were supplied by GIBCO/BRL and Life Technologies (Grand Island, NY). Cell membrane pellets were prepared and receptor autoradiography was performed on pellet sections (mounted on microscope slides), as described in detail previously . For each of the tested compounds, complete displacement experiments were performed with the universal somatostatin radioligand [125I]-[Leu8,D-Trp22,Trp25]-somatostatin-28 using increasing concentrations of the MetalloIII-DOTA-peptide ranging from 0.1 to 1,000nmol/l. Somatostatin-28 was run in parallel as control using the same increasing concentrations. IC50values were calculated after quantification of the data using a computer-assisted image processing system. Tissue standards (autoradiographic [125I] microscales, Amersham, UK) containing known amounts of isotopes, cross-calibrated to tissue-equivalent ligand concentrations, were used for quantification . The concentrations of the peptide solutions were measured by UV spectroscopy (NOC-ATE, 280nm = 9,855cm-1mol-1dm3, BOC-ATE, 280nm = 7,570cm-1mol-1dm3, TOC, 280nm> = 6,849cm-1mol-1dm3, NOC,280nm> = 9,850cm-1mol-1dm3)."	CHO-K1 and CCL39 cellsSSRT4	REF00165; REF003281
PEP00105	Ga-DOTA-TATEa octreotide	IC50	300 &plusmn; 140 nmol/L	"CHO-K1 and CCL39 cells stably expressing human sst1-5 (hsst1-5) were grown as described previously . All culture reagents were supplied by GIBCO/BRL and Life Technologies (Grand Island, NY). Cell membrane pellets were prepared and receptor autoradiography was performed on pellet sections (mounted on microscope slides), as described in detail previously . For each of the tested compounds, complete displacement experiments were performed with the universal somatostatin radioligand [125I]-[Leu8,D-Trp22,Trp25]-somatostatin-28 using increasing concentrations of the MetalloIII-DOTA-peptide ranging from 0.1 to 1,000nmol/l. Somatostatin-28 was run in parallel as control using the same increasing concentrations. IC50values were calculated after quantification of the data using a computer-assisted image processing system. Tissue standards (autoradiographic [125I] microscales, Amersham, UK) containing known amounts of isotopes, cross-calibrated to tissue-equivalent ligand concentrations, were used for quantification . The concentrations of the peptide solutions were measured by UV spectroscopy (NOC-ATE, 280nm = 9,855cm-1mol-1dm3, BOC-ATE, 280nm = 7,570cm-1mol-1dm3, TOC, 280nm> = 6,849cm-1mol-1dm3, NOC,280nm> = 9,850cm-1mol-1dm3)."	CHO-K1 and CCL39 cellsSSRT4	REF00165; REF003281
PEP00105	Ga-DOTA-TATEa octreotide	IC50	&gt; 1000 nmol/L	"CHO-K1 and CCL39 cells stably expressing human sst1-5 (hsst1-5) were grown as described previously . All culture reagents were supplied by GIBCO/BRL and Life Technologies (Grand Island, NY). Cell membrane pellets were prepared and receptor autoradiography was performed on pellet sections (mounted on microscope slides), as described in detail previously . For each of the tested compounds, complete displacement experiments were performed with the universal somatostatin radioligand [125I]-[Leu8,D-Trp22,Trp25]-somatostatin-28 using increasing concentrations of the MetalloIII-DOTA-peptide ranging from 0.1 to 1,000nmol/l. Somatostatin-28 was run in parallel as control using the same increasing concentrations. IC50values were calculated after quantification of the data using a computer-assisted image processing system. Tissue standards (autoradiographic [125I] microscales, Amersham, UK) containing known amounts of isotopes, cross-calibrated to tissue-equivalent ligand concentrations, were used for quantification . The concentrations of the peptide solutions were measured by UV spectroscopy (NOC-ATE, 280nm = 9,855cm-1mol-1dm3, BOC-ATE, 280nm = 7,570cm-1mol-1dm3, TOC, 280nm> = 6,849cm-1mol-1dm3, NOC,280nm> = 9,850cm-1mol-1dm3)."	CHO-K1 and CCL39 cellsSSRT3	REF00165; REF003281
_PEP00105	Y-DOTA-TATEa octreotide	IC50	&gt; 1000 nmol/L	"CHO-K1 and CCL39 cells stably expressing human sst1-5 (hsst1-5) were grown as described previously . All culture reagents were supplied by GIBCO/BRL and Life Technologies (Grand Island, NY). Cell membrane pellets were prepared and receptor autoradiography was performed on pellet sections (mounted on microscope slides), as described in detail previously . For each of the tested compounds, complete displacement experiments were performed with the universal somatostatin radioligand [125I]-[Leu8,D-Trp22,Trp25]-somatostatin-28 using increasing concentrations of the MetalloIII-DOTA-peptide ranging from 0.1 to 1,000nmol/l. Somatostatin-28 was run in parallel as control using the same increasing concentrations. IC50values were calculated after quantification of the data using a computer-assisted image processing system. Tissue standards (autoradiographic [125I] microscales, Amersham, UK) containing known amounts of isotopes, cross-calibrated to tissue-equivalent ligand concentrations, were used for quantification . The concentrations of the peptide solutions were measured by UV spectroscopy (NOC-ATE, 280nm = 9,855cm-1mol-1dm3, BOC-ATE, 280nm = 7,570cm-1mol-1dm3, TOC, 280nm> = 6,849cm-1mol-1dm3, NOC,280nm> = 9,850cm-1mol-1dm3)."	CHO-K1 and CCL39 cellsSSRT3	REF00165; REF003281
PEP00105	Y-DOTA-TATEa octreotide	IC50	1.6 &plusmn; 0.4 nmol/L	"CHO-K1 and CCL39 cells stably expressing human sst1-5 (hsst1-5) were grown as described previously . All culture reagents were supplied by GIBCO/BRL and Life Technologies (Grand Island, NY). Cell membrane pellets were prepared and receptor autoradiography was performed on pellet sections (mounted on microscope slides), as described in detail previously . For each of the tested compounds, complete displacement experiments were performed with the universal somatostatin radioligand [125I]-[Leu8,D-Trp22,Trp25]-somatostatin-28 using increasing concentrations of the MetalloIII-DOTA-peptide ranging from 0.1 to 1,000nmol/l. Somatostatin-28 was run in parallel as control using the same increasing concentrations. IC50values were calculated after quantification of the data using a computer-assisted image processing system. Tissue standards (autoradiographic [125I] microscales, Amersham, UK) containing known amounts of isotopes, cross-calibrated to tissue-equivalent ligand concentrations, were used for quantification . The concentrations of the peptide solutions were measured by UV spectroscopy (NOC-ATE, 280nm = 9,855cm-1mol-1dm3, BOC-ATE, 280nm = 7,570cm-1mol-1dm3, TOC, 280nm> = 6,849cm-1mol-1dm3, NOC,280nm> = 9,850cm-1mol-1dm3)."	CHO-K1 and CCL39 cellsSSRT2	REF00165; REF003281
PEP00105	Ga-DOTA-TATEa octreotide	IC50	0.20 &plusmn; 0.04 nmol/L	"CHO-K1 and CCL39 cells stably expressing human sst1-5 (hsst1-5) were grown as described previously . All culture reagents were supplied by GIBCO/BRL and Life Technologies (Grand Island, NY). Cell membrane pellets were prepared and receptor autoradiography was performed on pellet sections (mounted on microscope slides), as described in detail previously . For each of the tested compounds, complete displacement experiments were performed with the universal somatostatin radioligand [125I]-[Leu8,D-Trp22,Trp25]-somatostatin-28 using increasing concentrations of the MetalloIII-DOTA-peptide ranging from 0.1 to 1,000nmol/l. Somatostatin-28 was run in parallel as control using the same increasing concentrations. IC50values were calculated after quantification of the data using a computer-assisted image processing system. Tissue standards (autoradiographic [125I] microscales, Amersham, UK) containing known amounts of isotopes, cross-calibrated to tissue-equivalent ligand concentrations, were used for quantification . The concentrations of the peptide solutions were measured by UV spectroscopy (NOC-ATE, 280nm = 9,855cm-1mol-1dm3, BOC-ATE, 280nm = 7,570cm-1mol-1dm3, TOC, 280nm> = 6,849cm-1mol-1dm3, NOC,280nm> = 9,850cm-1mol-1dm3)."	CHO-K1 and CCL39 cellsSSRT2	REF00165; REF003281
PEP00105	Ga-DOTA-TATEa octreotide	IC50	&gt; 10000 nmol/L	"CHO-K1 and CCL39 cells stably expressing human sst1-5 (hsst1-5) were grown as described previously . All culture reagents were supplied by GIBCO/BRL and Life Technologies (Grand Island, NY). Cell membrane pellets were prepared and receptor autoradiography was performed on pellet sections (mounted on microscope slides), as described in detail previously . For each of the tested compounds, complete displacement experiments were performed with the universal somatostatin radioligand [125I]-[Leu8,D-Trp22,Trp25]-somatostatin-28 using increasing concentrations of the MetalloIII-DOTA-peptide ranging from 0.1 to 1,000nmol/l. Somatostatin-28 was run in parallel as control using the same increasing concentrations. IC50values were calculated after quantification of the data using a computer-assisted image processing system. Tissue standards (autoradiographic [125I] microscales, Amersham, UK) containing known amounts of isotopes, cross-calibrated to tissue-equivalent ligand concentrations, were used for quantification . The concentrations of the peptide solutions were measured by UV spectroscopy (NOC-ATE, 280nm = 9,855cm-1mol-1dm3, BOC-ATE, 280nm = 7,570cm-1mol-1dm3, TOC, 280nm> = 6,849cm-1mol-1dm3, NOC,280nm> = 9,850cm-1mol-1dm3)."	CHO-K1 and CCL39 cellsSSRT1	REF00165; REF003281
_PEP00105	Y-DOTA-TATEa octreotide	IC50	&gt; 10000 nmol/L	"CHO-K1 and CCL39 cells stably expressing human sst1-5 (hsst1-5) were grown as described previously . All culture reagents were supplied by GIBCO/BRL and Life Technologies (Grand Island, NY). Cell membrane pellets were prepared and receptor autoradiography was performed on pellet sections (mounted on microscope slides), as described in detail previously . For each of the tested compounds, complete displacement experiments were performed with the universal somatostatin radioligand [125I]-[Leu8,D-Trp22,Trp25]-somatostatin-28 using increasing concentrations of the MetalloIII-DOTA-peptide ranging from 0.1 to 1,000nmol/l. Somatostatin-28 was run in parallel as control using the same increasing concentrations. IC50values were calculated after quantification of the data using a computer-assisted image processing system. Tissue standards (autoradiographic [125I] microscales, Amersham, UK) containing known amounts of isotopes, cross-calibrated to tissue-equivalent ligand concentrations, were used for quantification . The concentrations of the peptide solutions were measured by UV spectroscopy (NOC-ATE, 280nm = 9,855cm-1mol-1dm3, BOC-ATE, 280nm = 7,570cm-1mol-1dm3, TOC, 280nm> = 6,849cm-1mol-1dm3, NOC,280nm> = 9,850cm-1mol-1dm3)."	CHO-K1 and CCL39 cellsSSRT1	REF00165; REF003281
PEP00030	PSMA-617	Equilibrium dissociation constant	2.34 &plusmn; 2.94 nM	NAALADase assay	LNCaP cells	REF00134;REF003301
PEP00163	c[DKP-RGD]	IC50	&gt; 5 nM	IC50values were calculated as the concentration of compound required for 50% inhibition of biotinylated vitronectin binding	&alpha;v&beta;5 receptor	REF00069; REF003291
PEP00163	c[DKP-RGD]	IC50	26.4&plusmn;3.7 nM	IC50values were calculated as the concentration of compound required for 50% inhibition of biotinylated vitronectin binding	&alpha;v&beta;3 receptor	REF00069; REF003291
PEP00116	HER2-targeting peptide P1	K<sub>D</sub>	5.7 &mu;M	"The HER2 recombinant protein was initially coupled to Chip CM5 by amide formation reaction using EDC/NHS. Different peptide concentrations (50, 25, 12.5, 6.25, and 3.125 &mu;M) dissolved in PBST buffer flowed across the surface of the protein-coupled chip, and real-time binding signals were recorded and analyzed."	Protein-coupled chip in vitro	REF00312
PEP00117	<sup>D</sup>VAP	K<sub>D</sub>	18.81 nM	"Surface plasmon resonance (SPR) experiments were carried out using a Biacore T200 system (GE Healthcare) to examine whether peptides retain their binding affinity with GRP78 protein and Dopamine receptor protein. After the recombinant receptor proteins were coupled to the CM5 chip, peptides were dissolved in PBS and then injected into the system to record resonance changes. KD (equilibrium dissociation constant) values were calculated using the Biacore software."	GRP78 protein in vitro	REF00308
PEP00179	DPI-4452	K<sub>D</sub>	0.25 nM	"Recombinant CA proteins (Sino Biologic) were immobilized on Biacore CM5 sensor chips or biotin CAPture chips (Biacore). DPI-4452 binding was measured using the Biacore Liquid System (Biacore), and binding kinetic parameters were calculated."	Biacore CM5 sensor chips in vitro	REF00324
PEP00179	DPI-4452	Dissociation half-life	99 min	"Recombinant CA proteins (Sino Biologic) were immobilized on Biacore CM5 sensor chips or biotin CAPture chips (Biacore). DPI-4452 binding was measured using the Biacore Liquid System (Biacore), and binding kinetic parameters were calculated."	Biacore CM5 sensor chips in vitro	REF00324
PEP00026	DYEMHLWWGTEL	K<sub>D</sub>	0.38 &mu;M	A fluorescence polarization test was performed to measure the binding affinity between PS conjugates and GPC3.	GPC3 protein in vitro	REF00289
PEP00066	KKKRLNVGGTYFLTTRQ	Fluorescence polarization	0.08	A fluorescence polarization test was performed to measure the binding affinity between PS conjugates and GPC3.	GPC3 protein in vitro	REF00289
PEP00026	DYEMHLWWGTEL	Fluorescence polarization	0.06	A fluorescence polarization test was performed to measure the binding affinity between PS conjugates and GPC3.	GPC3 protein in vitro	REF00289
PEP00125	RLNVGGTYFLTTRQ	Fluorescence polarization	0.04	A fluorescence polarization test was performed to measure the binding affinity between PS conjugates and GPC3.	GPC3 protein in vitro	REF00289
PEP00025	DHLASLWWGTEL	Fluorescence polarization	0.02	A fluorescence polarization test was performed to measure the binding affinity between PS conjugates and GPC3.	GPC3 protein in vitro	REF00289
PEP00030	PSMA-617	IC50	11.10 &plusmn; 0.80 nM	Assays were carried out by incubating PSMA-positive cells with 0.2 nM MIP-1095 in the presence of 1 &mu;M PSMA-617.	PC3-PIP cell	REF00277
PEP00148	rL-A9	Binding free energy	-22.2 kJ/mol	"The peptides were prepared and energy minimized using the ACD ChemSketch suite (ACD/ChemSketch for Academic and Personal Use: ACD/Labs.com, 2018). The protein was prepared by adding hydrogens using AutoDockTools 4. (27) The active site cavity was selected and used a grid box of 20 20 20 for docking, spanning the peptide binding region on the HER2 surface. Molecular docking studies were performed using AutoDock Vina 1.1 with its scoring functions. (28) The top 10 peptide poses were generated after docking. The binding free energies of the best 10 ligand poses bound to the receptor were obtained, and these poses were analyzed."	The model of HER2-DIVMP/peptide complexes	REF003361
PEP00020	TAR	K<sub>D</sub>	33.97 nM	"The surface plasmon resonance (SPR) detection technique was used to determine the binding affinity of TAR peptide to NRP-1 by Biacore T200 instrument (GE). First, the purified NRP-1 protein was immobilized on the CM5 chip. Then, using HBS-EP as a running buffer, a gradient-diluted TAR peptide solution was configured to flow through the surface of the chip for binding and dissociation. Finally, the data were analyzed using the Biacore T200 evaluation software 2.0.1."	Chip CM5 in the vitro	REF00255
PEP00115	P1GCGT1	Polar solvation energy	1418 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-IV)	REF00244
PEP00114	P1GCGCGT1	Polar solvation energy	1112.37 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-IV)	REF00244
PEP00114	P1GCGCGT1	SASA energy	-53.81 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-IV)	REF00244
PEP00115	P1GCGT1	SASA energy	-68.33 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-IV)	REF00244
PEP00115	P1GCGT1	Binding energy	-208.96 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-IV)	REF00244
PEP00114	P1GCGCGT1	Binding energy	-243.65 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-IV)	REF00244
PEP00114	P1GCGCGT1	Electrostatic energy	-278.26 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-IV)	REF00244
PEP00115	P1GCGT1	Electrostatic energy	-301.04 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-IV)	REF00244
PEP00114	P1GCGCGT1	Van der Waals energy	-1023.85 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-IV)	REF00244
PEP00115	P1GCGT1	Van der Waals energy	-1257.58 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-IV)	REF00244
PEP00115	P1GCGT1	Polar solvation energy	963.88 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-II)	REF00244
PEP00114	P1GCGCGT1	Polar solvation energy	561.31 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-II)	REF00244
PEP00114	P1GCGCGT1	SASA energy	-46.17 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-II)	REF00244
PEP00115	P1GCGT1	SASA energy	-57.47 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-II)	REF00244
PEP00115	P1GCGT1	Binding energy	-162.14 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-II)	REF00244
PEP00114	P1GCGCGT1	Binding energy	-181.51 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-II)	REF00244
PEP00115	P1GCGT1	Electrostatic energy	-263.26 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-II)	REF00244
PEP00114	P1GCGCGT1	Electrostatic energy	-304.69 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-II)	REF00244
PEP00114	P1GCGCGT1	Van der Waals energy	-391.96 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-II)	REF00244
PEP00115	P1GCGT1	Van der Waals energy	-805.29 kJ/mol	"To further study the interaction between peptides and HER2 protein, the binding free energy was calculated for each complex using the MMPBSA method."	MMPBSA method (HER2-II)	REF00244
PEP00114	P1GCGCGT1	K<sub>D</sub>	385 nM	"The HER2 recombinant protein was initially coupled to Chip CM5 by amide formation reaction using EDC/NHS. Different peptide concentrations (50, 25, 12.5, 6.25, and 3.125 &mu;M) dissolved in PBST buffer flowed across the surface of the protein-coupled chip, and real-time binding signals were recorded and analyzed. The Biacore evaluation software was used to calculate the dissociation constant (KD) according to association-dissociation curves at different peptide concentrations."	Chip CM5 in the vitro	REF00244
PEP00115	P1GCGT1	K<sub>D</sub>	151 nM	"The HER2 recombinant protein was initially coupled to Chip CM5 by amide formation reaction using EDC/NHS. Different peptide concentrations (50, 25, 12.5, 6.25, and 3.125 &mu;M) dissolved in PBST buffer flowed across the surface of the protein-coupled chip, and real-time binding signals were recorded and analyzed. The Biacore evaluation software was used to calculate the dissociation constant (KD) according to association-dissociation curves at different peptide concentrations."	Chip CM5 in the vitro	REF00244
PEP00171	Bicycle toxin conjugate precursor	K<sub>D</sub>	2.5 nM	KD determined by surface plasmon resonance (SPR)	CM5 (GE Healthcare) or CMD5000 (Xantec) chip in the vitro(Nectin-4 of the parent Bicycle)	REF00236
PEP00171	Bicycle toxin conjugate precursor	K<sub>D</sub>	12.9 nM	KD determined by surface plasmon resonance (SPR)	CM5 (GE Healthcare) or CMD5000 (Xantec) chip in the vitro(endogenous Nectin-4 on cells)	REF00236
PEP00017	Peptide 1131	Fluorescence intensity	2000	"For the fluorescence-linked immunosorbent assay (FLISA), flat-bottom 96-well cell culture plates (Thermo Fisher Scientific, Waltham, MA, USA) were coated with 10 &mu;g/mL KK-LC-1 protein solution at 4 &deg;C overnight and then blocked with 1% BSA-PBS at room temperature for 1 h. The plates were washed with PBS containing 0.1% Tween 20 (0.1% PBST). Three-fold dilutions of FITC-labeled 1131-MMAE, 1131 peptide and the non-targeting control CG7C-MMAE were added and incubated at room temperature for 2 h. The plates were washed again and the fluorescence intensity was measured with a multimode microplate reader (Tecan, Mendov, Switzerland). The excitation wavelength was 485 nm and emission wavelength was 535 nm."	10 &mu;g/mL KK-LC-1 protein solution at 4 C overnight	REF00226
PEP00008	CCKIGLFRWR	IC50	51.73 &mu;M	In vitro collagenase inhibition experiments	.	REF00112
PEP00170	BCY6099	K<sub>D</sub>	5.7 &plusmn; 0.9  nmol/L	Binding affinities were determined using a fluorescence polarization competition assay and surface plasmon resonance assays using conventional methods.	.	REF00110
PEP00055	Xenopus glucagon-like peptide-1 (xGLP-1)	EC50	0.045 &plusmn; 0.011 nM	"The relative HSA binding abilities of liraglutide,2a-d, and3a-dwere determined using high-performance affinity chromatography (HPAC) method as previously described with slight changes [33]. Briefly, chromatographic separation was performed on Agilent HPLC (mode 1260) using an immobilized HSA column (CHIRALPAK-HSA, 2mm50mm, 5&mu;m, Chiral Technologies Europe). The mobile phase was potassium phosphate buffer (pH 7.0, 20mM) containing 25% 2-propanol. The column was kept at 25&deg;C and the wavelength for detection was 214nm. The retention times (tR) for each peptide were determined in triplicate. The value of dead time (to) was determined by injecting acyclovir (non-binding compound)."	HEK-293 cell	REF00109
_PEP00055	Xenopus glucagon-like peptide-1 (xGLP-1)	EC50	0.045 &plusmn; 0.011 nM	"The relative HSA binding abilities of liraglutide,2a-d, and3a-dwere determined using high-performance affinity chromatography (HPAC) method as previously described with slight changes [33]. Briefly, chromatographic separation was performed on Agilent HPLC (mode 1260) using an immobilized HSA column (CHIRALPAK-HSA, 2mm50mm, 5&mu;m, Chiral Technologies Europe). The mobile phase was potassium phosphate buffer (pH 7.0, 20mM) containing 25% 2-propanol. The column was kept at 25&deg;C and the wavelength for detection was 214nm. The retention times (tR) for each peptide were determined in triplicate. The value of dead time (to) was determined by injecting acyclovir (non-binding compound)."	HEK-293 cell	REF00109
_PEP00055	Xenopus glucagon-like peptide-1 (xGLP-1)	EC50	0.045 &plusmn; 0.011 nM	"The relative HSA binding abilities of liraglutide,2a-d, and3a-dwere determined using high-performance affinity chromatography (HPAC) method as previously described with slight changes [33]. Briefly, chromatographic separation was performed on Agilent HPLC (mode 1260) using an immobilized HSA column (CHIRALPAK-HSA, 2mm50mm, 5&mu;m, Chiral Technologies Europe). The mobile phase was potassium phosphate buffer (pH 7.0, 20mM) containing 25% 2-propanol. The column was kept at 25&deg;C and the wavelength for detection was 214nm. The retention times (tR) for each peptide were determined in triplicate. The value of dead time (to) was determined by injecting acyclovir (non-binding compound)."	HEK-293 cell	REF00109
_PEP00055	Xenopus glucagon-like peptide-1 (xGLP-1)	EC50	0.045 &plusmn; 0.011 nM	"The relative HSA binding abilities of liraglutide,2a-d, and3a-dwere determined using high-performance affinity chromatography (HPAC) method as previously described with slight changes [33]. Briefly, chromatographic separation was performed on Agilent HPLC (mode 1260) using an immobilized HSA column (CHIRALPAK-HSA, 2mm50mm, 5&mu;m, Chiral Technologies Europe). The mobile phase was potassium phosphate buffer (pH 7.0, 20mM) containing 25% 2-propanol. The column was kept at 25&deg;C and the wavelength for detection was 214nm. The retention times (tR) for each peptide were determined in triplicate. The value of dead time (to) was determined by injecting acyclovir (non-binding compound)."	HEK-293 cell	REF00109
_PEP00055	Xenopus glucagon-like peptide-1 (xGLP-1)	EC50	0.045 &plusmn; 0.011 nM	"The relative HSA binding abilities of liraglutide,2a-d, and3a-dwere determined using high-performance affinity chromatography (HPAC) method as previously described with slight changes [33]. Briefly, chromatographic separation was performed on Agilent HPLC (mode 1260) using an immobilized HSA column (CHIRALPAK-HSA, 2mm50mm, 5&mu;m, Chiral Technologies Europe). The mobile phase was potassium phosphate buffer (pH 7.0, 20mM) containing 25% 2-propanol. The column was kept at 25&deg;C and the wavelength for detection was 214nm. The retention times (tR) for each peptide were determined in triplicate. The value of dead time (to) was determined by injecting acyclovir (non-binding compound)."	HEK-293 cell	REF00109
_PEP00055	Xenopus glucagon-like peptide-1 (xGLP-1)	EC50	0.045 &plusmn; 0.011 nM	"The relative HSA binding abilities of liraglutide,2a-d, and3a-dwere determined using high-performance affinity chromatography (HPAC) method as previously described with slight changes [33]. Briefly, chromatographic separation was performed on Agilent HPLC (mode 1260) using an immobilized HSA column (CHIRALPAK-HSA, 2mm50mm, 5&mu;m, Chiral Technologies Europe). The mobile phase was potassium phosphate buffer (pH 7.0, 20mM) containing 25% 2-propanol. The column was kept at 25&deg;C and the wavelength for detection was 214nm. The retention times (tR) for each peptide were determined in triplicate. The value of dead time (to) was determined by injecting acyclovir (non-binding compound)."	HEK-293 cell	REF00109
_PEP00055	Xenopus glucagon-like peptide-1 (xGLP-1)	EC50	0.045 &plusmn; 0.011 nM	"The relative HSA binding abilities of liraglutide,2a-d, and3a-dwere determined using high-performance affinity chromatography (HPAC) method as previously described with slight changes [33]. Briefly, chromatographic separation was performed on Agilent HPLC (mode 1260) using an immobilized HSA column (CHIRALPAK-HSA, 2mm50mm, 5&mu;m, Chiral Technologies Europe). The mobile phase was potassium phosphate buffer (pH 7.0, 20mM) containing 25% 2-propanol. The column was kept at 25&deg;C and the wavelength for detection was 214nm. The retention times (tR) for each peptide were determined in triplicate. The value of dead time (to) was determined by injecting acyclovir (non-binding compound)."	HEK-293 cell	REF00109
_PEP00055	Xenopus glucagon-like peptide-1 (xGLP-1)	EC50	0.045 &plusmn; 0.011 nM	"The relative HSA binding abilities of liraglutide,2a-d, and3a-dwere determined using high-performance affinity chromatography (HPAC) method as previously described with slight changes [33]. Briefly, chromatographic separation was performed on Agilent HPLC (mode 1260) using an immobilized HSA column (CHIRALPAK-HSA, 2mm50mm, 5&mu;m, Chiral Technologies Europe). The mobile phase was potassium phosphate buffer (pH 7.0, 20mM) containing 25% 2-propanol. The column was kept at 25&deg;C and the wavelength for detection was 214nm. The retention times (tR) for each peptide were determined in triplicate. The value of dead time (to) was determined by injecting acyclovir (non-binding compound)."	HEK-293 cell	REF00109
_PEP00055	Xenopus glucagon-like peptide-1 (xGLP-1)	EC50	0.045 &plusmn; 0.011 nM	"The relative HSA binding abilities of liraglutide,2a-d, and3a-dwere determined using high-performance affinity chromatography (HPAC) method as previously described with slight changes [33]. Briefly, chromatographic separation was performed on Agilent HPLC (mode 1260) using an immobilized HSA column (CHIRALPAK-HSA, 2mm50mm, 5&mu;m, Chiral Technologies Europe). The mobile phase was potassium phosphate buffer (pH 7.0, 20mM) containing 25% 2-propanol. The column was kept at 25&deg;C and the wavelength for detection was 214nm. The retention times (tR) for each peptide were determined in triplicate. The value of dead time (to) was determined by injecting acyclovir (non-binding compound)."	HEK-293 cell	REF00109
PEP00096	NALRDQTGLKNPVQLARAVC	MTT activity	90%	"Relative amounts of mitochondrial activity were quantified as an indirect measure of cell proliferation using the MTT assay (Promega). All cell lines were seeded at 3x10<sup>3</sup> cells/mL into 96-well plates. After 24h, cells were treated with serially-diluted concentrations of NT-peptide control, A20FMDV2, SG3199, SG3511 or SG3299 (0-500 nM, n=6 replicates/treatment) in serum-free media. Three biological repeats were performed. After 72 h, cells were subject to the MTT assay. Briefly, cell culture media was removed from each well and 100 &mu;l of MTT reagent was added per well. After 1h at 37&deg;C, MTT solution was replaced with 200&mu;l DMSO and fluorescence measured at 550nm wavelength. Data were plotted relative to PBS (n=6, error bars represent standard deviation)."	Capan-1 cell	REF00096
PEP00097	A20FMDV2	MTT activity	72%	"Relative amounts of mitochondrial activity were quantified as an indirect measure of cell proliferation using the MTT assay (Promega). All cell lines were seeded at 3x10<sup>3</sup> cells/mL into 96-well plates. After 24h, cells were treated with serially-diluted concentrations of NT-peptide control, A20FMDV2, SG3199, SG3511 or SG3299 (0-500 nM, n=6 replicates/treatment) in serum-free media. Three biological repeats were performed. After 72 h, cells were subject to the MTT assay. Briefly, cell culture media was removed from each well and 100 &mu;l of MTT reagent was added per well. After 1h at 37&deg;C, MTT solution was replaced with 200&mu;l DMSO and fluorescence measured at 550nm wavelength. Data were plotted relative to PBS (n=6, error bars represent standard deviation)."	Capan-1 cell	REF00096
PEP00096	NALRDQTGLKNPVQLARAVC	MTT activity	92%	"Relative amounts of mitochondrial activity were quantified as an indirect measure of cell proliferation using the MTT assay (Promega). All cell lines were seeded at 3x10<sup>3</sup> cells/mL into 96-well plates. After 24h, cells were treated with serially-diluted concentrations of NT-peptide control, A20FMDV2, SG3199, SG3511 or SG3299 (0-500 nM, n=6 replicates/treatment) in serum-free media. Three biological repeats were performed. After 72 h, cells were subject to the MTT assay. Briefly, cell culture media was removed from each well and 100 &mu;l of MTT reagent was added per well. After 1h at 37&deg;C, MTT solution was replaced with 200&mu;l DMSO and fluorescence measured at 550nm wavelength. Data were plotted relative to PBS (n=6, error bars represent standard deviation)."	A375P&beta;6 cell	REF00096
PEP00097	A20FMDV2	MTT activity	80%	"Relative amounts of mitochondrial activity were quantified as an indirect measure of cell proliferation using the MTT assay (Promega). All cell lines were seeded at 3x10<sup>3</sup> cells/mL into 96-well plates. After 24h, cells were treated with serially-diluted concentrations of NT-peptide control, A20FMDV2, SG3199, SG3511 or SG3299 (0-500 nM, n=6 replicates/treatment) in serum-free media. Three biological repeats were performed. After 72 h, cells were subject to the MTT assay. Briefly, cell culture media was removed from each well and 100 &mu;l of MTT reagent was added per well. After 1h at 37&deg;C, MTT solution was replaced with 200&mu;l DMSO and fluorescence measured at 550nm wavelength. Data were plotted relative to PBS (n=6, error bars represent standard deviation)."	A375P&beta;6 cell	REF00096
PEP00096	NALRDQTGLKNPVQLARAVC	MTT activity	89%	"Relative amounts of mitochondrial activity were quantified as an indirect measure of cell proliferation using the MTT assay (Promega). All cell lines were seeded at 3x10<sup>3</sup> cells/mL into 96-well plates. After 24h, cells were treated with serially-diluted concentrations of NT-peptide control, A20FMDV2, SG3199, SG3511 or SG3299 (0-500 nM, n=6 replicates/treatment) in serum-free media. Three biological repeats were performed. After 72 h, cells were subject to the MTT assay. Briefly, cell culture media was removed from each well and 100 &mu;l of MTT reagent was added per well. After 1h at 37&deg;C, MTT solution was replaced with 200&mu;l DMSO and fluorescence measured at 550nm wavelength. Data were plotted relative to PBS (n=6, error bars represent standard deviation)."	A375Ppuro cell	REF00096
PEP00097	A20FMDV2	MTT activity	78%	"Relative amounts of mitochondrial activity were quantified as an indirect measure of cell proliferation using the MTT assay (Promega). All cell lines were seeded at 3x10<sup>3</sup> cells/mL into 96-well plates. After 24h, cells were treated with serially-diluted concentrations of NT-peptide control, A20FMDV2, SG3199, SG3511 or SG3299 (0-500 nM, n=6 replicates/treatment) in serum-free media. Three biological repeats were performed. After 72 h, cells were subject to the MTT assay. Briefly, cell culture media was removed from each well and 100 &mu;l of MTT reagent was added per well. After 1h at 37&deg;C, MTT solution was replaced with 200&mu;l DMSO and fluorescence measured at 550nm wavelength. Data were plotted relative to PBS (n=6, error bars represent standard deviation)."	A375Ppuro cell	REF00096
PEP00159	"[K4(C-&beta;A-),F7,L17,P34]-hNPY"	EC50	8.5 nM	"The receptor activation, selectivity, and internalization were investigated to ensure that the attachment of the cleavable linker and tesa did not alter the behavior of NPY1R-preferring carrier peptide [F7, P34]-NPY. The activation of the human Y-receptors was tested using Ca2+-flux assays in COS-7 cells stably expressing one specific Y-receptor subtype (NPY1/2/4/5R) and chimeric G protein (6Gaqi4-myr), opening the Ca2+ channels upon receptor activation"	COS-7 cells	REF00088
PEP00159	"[K4(C-&beta;A-),F7,L17,P34]-hNPY"	EC50	32 (7.5&plusmn;0.1) nM	"The receptor activation, selectivity, and internalization were investigated to ensure that the attachment of the cleavable linker and tesa did not alter the behavior of NPY1R-preferring carrier peptide [F7, P34]-NPY. The activation of the human Y-receptors was tested using Ca2+-flux assays in COS-7 cells stably expressing one specific Y-receptor subtype (NPY1/2/4/5R) and chimeric G protein (6Gaqi4-myr), opening the Ca2+ channels upon receptor activation"	COS-7 cells	REF00088
PEP00159	"[K4(C-&beta;A-),F7,L17,P34]-hNPY"	EC50	0.3 nM	"The receptor activation, selectivity, and internalization were investigated to ensure that the attachment of the cleavable linker and tesa did not alter the behavior of NPY1R-preferring carrier peptide [F7, P34]-NPY. The activation of the human Y-receptors was tested using Ca2+-flux assays in COS-7 cells stably expressing one specific Y-receptor subtype (NPY1/2/4/5R) and chimeric G protein (6Gaqi4-myr), opening the Ca2+ channels upon receptor activation"	COS-7 cells	REF00088
_PEP00159	"[K4(C-&beta;A-),F7,L17,P34]-hNPY"	EC50	0.3 nM	"The receptor activation, selectivity, and internalization were investigated to ensure that the attachment of the cleavable linker and tesa did not alter the behavior of NPY1R-preferring carrier peptide [F7, P34]-NPY. The activation of the human Y-receptors was tested using Ca2+-flux assays in COS-7 cells stably expressing one specific Y-receptor subtype (NPY1/2/4/5R) and chimeric G protein (6Gaqi4-myr), opening the Ca2+ channels upon receptor activation"	COS-7 cells	REF00088
PEP00162	Angiopep-2	K<sub>D</sub>	36.8 nM	We therefore measured the binding kinetics of the peptide to LRP1 in the format of protein fusion.	Low-density LRP1	REF00077
PEP00140	M1	K<sub>D</sub>	11.6 nM	We therefore measured the binding kinetics of the peptide to LRP1 in the format of protein fusion.	Low-density LRP1	REF00077
PEP00030	PSMA-617	Administered target activity	6-7.5 MBq	.	.	REF00076
PEP00038	E1-3	Abs 410nm	0.65	"Medulloblastoma cells (DAOY) were plated into 96-multiwell ELISA plates (1 10<sup>3</sup> cells/well) the day prior to the assay. Cells were incubated in fresh culture medium without serum for 1 h at 37 &deg;C and then fixed with freshly prepared 4% paraformaldehyde for 20 min at room temperature. Cells were washed three times in PBS and blocked for 1 h at room temperature in PBS containing 2% nonfat skim milk powder. The selected phage clones and a negative control M13KE phage were added (5 1010 pfu/well) individually to the cells and incubated for 90 min at room temperature. The phages were removed and cells washed in PBS containing 0.05% Tween. Anti-M13 antibody conjugated to horseradish peroxidase (HRP) was added to each well and incubated at room temperature for 1 h. Cells were washed with PBS containing 0.05% Tween and incubated with 2,2-azino-bis (3-ethylbenzothiazoline-6 sulfonic acid, ABTS) for 30 min at room temperature. The color reaction was stopped using HCl and the optimal density (OD) for each sample was measured at 410 nm using a microplate reader (PerkinElmer Victor3 plate reader)."	Medulloblastoma cells	REF00071
PEP00143	E1-7	Abs 410nm	0.05	"Medulloblastoma cells (DAOY) were plated into 96-multiwell ELISA plates (1 10<sup>3</sup> cells/well) the day prior to the assay. Cells were incubated in fresh culture medium without serum for 1 h at 37 &deg;C and then fixed with freshly prepared 4% paraformaldehyde for 20 min at room temperature. Cells were washed three times in PBS and blocked for 1 h at room temperature in PBS containing 2% nonfat skim milk powder. The selected phage clones and a negative control M13KE phage were added (5 1010 pfu/well) individually to the cells and incubated for 90 min at room temperature. The phages were removed and cells washed in PBS containing 0.05% Tween. Anti-M13 antibody conjugated to horseradish peroxidase (HRP) was added to each well and incubated at room temperature for 1 h. Cells were washed with PBS containing 0.05% Tween and incubated with 2,2-azino-bis (3-ethylbenzothiazoline-6 sulfonic acid, ABTS) for 30 min at room temperature. The color reaction was stopped using HCl and the optimal density (OD) for each sample was measured at 410 nm using a microplate reader (PerkinElmer Victor3 plate reader)."	Medulloblastoma cells	REF00071
PEP00164	c[DKP-RGD]-PEG<sub>4</sub>-sC18	IC50	15.3 &plusmn; 5.2 nM	"Human integrin receptors avb3 (R&D Systems, Minneapolis, MN, USA) and avb5 (EMD Millipore Corporation, Inc., Temecula, CA, USA) were diluted to 0.5 &mu;g/mL in coating buffer containing 20 mM Tris-HCl (pH 7.4), 150 mM NaCl, 1 mM MnCl2, 2 mM CaCl2, and 1 mM MgCl2. An aliquot of diluted receptor (100 &mu;L/well) was added to 96-well microtiter plates (Nunc MaxiSorp, Termo Fisher Scientific, Roskilde, DK) and incubated overnight at 4 &deg;C. The plates were incubated with blocking solution (coating buffer plus 1% bovine serum albumin) for additional 2 h at room temperature to block nonspecific binding. After washing 2 times with blocking solution, plates were incubated shaking in the dark for 3 h at room temperature, with various concentrations (10<sup>-5</sup>-10<sup>-12</sup> M) of test compounds in the presence of 1 &mu;g/mL vitronectin (Molecular Innovations, Novi, MI, USA) biotinylated using an EZ-Link Sulfo-NHS-Biotinylation kit (Pierce, Rockford, IL, USA). After washing 3 times, the plates were incubated shaking for 1 h in the dark, at room temperature, with streptavidin-biotinylated peroxidase complex (Amersham Biosciences, Uppsala, Sweden). After washing 3 times with blocking solution, plates were incubated with 100 &mu;L/well of Substrate Reagent Solution (R&D Systems, Minneapolis, MN, USA) for 30 min shaking in the dark, before stopping the reaction with the addition of 50 &mu;L/well 2 N H2SO4. Absorbance at 415 nm was read in a Synergy HT Multi-Detection Microplate Reader (BioTek Instruments, Inc.). Each data point represents the average of triplicate wells; data analysis was carried out by nonlinear regression analysis with GraphPad Prism software. Each experiment was repeated in duplicate."	Biotinylated vitronectin(&alpha;v&beta;5)	REF00069
PEP00164	c[DKP-RGD]-PEG<sub>4</sub>-sC18	IC50	2.5 &plusmn; 0.2 nM	"Human integrin receptors avb3 (R&D Systems, Minneapolis, MN, USA) and avb5 (EMD Millipore Corporation, Inc., Temecula, CA, USA) were diluted to 0.5 &mu;g/mL in coating buffer containing 20 mM Tris-HCl (pH 7.4), 150 mM NaCl, 1 mM MnCl2, 2 mM CaCl2, and 1 mM MgCl2. An aliquot of diluted receptor (100 &mu;L/well) was added to 96-well microtiter plates (Nunc MaxiSorp, Termo Fisher Scientific, Roskilde, DK) and incubated overnight at 4 &deg;C. The plates were incubated with blocking solution (coating buffer plus 1% bovine serum albumin) for additional 2 h at room temperature to block nonspecific binding. After washing 2 times with blocking solution, plates were incubated shaking in the dark for 3 h at room temperature, with various concentrations (10<sup>-5</sup>-10<sup>-12</sup> M) of test compounds in the presence of 1 &mu;g/mL vitronectin (Molecular Innovations, Novi, MI, USA) biotinylated using an EZ-Link Sulfo-NHS-Biotinylation kit (Pierce, Rockford, IL, USA). After washing 3 times, the plates were incubated shaking for 1 h in the dark, at room temperature, with streptavidin-biotinylated peroxidase complex (Amersham Biosciences, Uppsala, Sweden). After washing 3 times with blocking solution, plates were incubated with 100 &mu;L/well of Substrate Reagent Solution (R&D Systems, Minneapolis, MN, USA) for 30 min shaking in the dark, before stopping the reaction with the addition of 50 &mu;L/well 2 N H2SO4. Absorbance at 415 nm was read in a Synergy HT Multi-Detection Microplate Reader (BioTek Instruments, Inc.). Each data point represents the average of triplicate wells; data analysis was carried out by nonlinear regression analysis with GraphPad Prism software. Each experiment was repeated in duplicate."	Biotinylated vitronectin(&alpha;v&beta;3)	REF00069
PEP00093	Chlorotoxin	Binding constant	240 nM	"Octet binding studies required biotinylation of Cltx and derived peptides for loading onto streptavidin biosensors. Trypsin, (Promega Cat# V5280) (&tide; 40 &mu;g/mL) was added to Cltx biotinylated at K27 or N-terminus (10 mg/mL) and incubated for 24 h at 37 &deg;C, pH 8.5. The resulting peptides were separated by preparative HPLC and peptide fragments were characterized by MALDI. Small linear Cltx-derived peptides were also synthesized by routine methods and were biotinylated at the N-terminus. In some cases, peptides were reduced with TCEP at pH 8 and the cysteine residues were capped using iodoacetamide."	Required biotinylation of Cltx	REF00067
PEP00152	[D-Lys6]-LH-RH	IC50	10.5&plusmn;0.2 nM	"Radioiodination of D-Tyr6-His5-GnRH, preparation of membrane homogenates from HEK 293 cells stably expressing the GnRH-R and binding of the GnRH-gemcitabine conjugates to the human GnRH-R was performed as described before [43,44]. In brief, aliquots of diluted membrane suspension (50 &mu;L) were added into tubes containing buffer B (25 mM HEPES containing 1 mM CaCl2, 10 mM MgCl2, 0.5% BSA, pH 7.4 at 4 &deg;C) and 100,000-120,000 cpm [125I]-D-Tyr6-His5-GnRH with or without increasing concentrations of GnRH-gemcitabine conjugates in a final volume of 0.2 mL. The mixtures were incubated at 4 &deg;C for 16-19 h and then filtered using a Brandel cell harvester through Whatman GF/C glass fiber filters, presoaked for 1-2 h in 0.5% polyethylenimine at 4 &deg;C. The filters were washed four times with 1.5 mL of ice-cold 50 mM Tris-HCl, pH 7.4 at 4 &deg;C. Filters were assessed for radioactivity in a gamma counter (LKB Wallac 1275 minigamma, 80% efficiency). The amount of membrane used was adjusted to ensure that the specific binding was always equal to or less than 10% of the total concentration of the added radioligand. Specific [125I]-D-Tyr6-His5-GnRH binding was defined as total binding less nonspecific binding in the presence of 1000 nM triptorelin (Bachem, Germany). Data for competition binding were analyzed by nonlinear regression analysis, using GraphPad Prism 4.0 (GraphPad Software, San Diego, CA). IC50 values were obtained by fitting the data from competition studies to a one-site competition model."	HEK 293 cells	REF00058
PEP00159	"[K4(C-&beta;A-),F7,L17,P34]-hNPY"	IC50	0.23 &plusmn; 0.05 nM	"Antiproliferative and cytotoxic effects, respectively, of the compounds were detected by using a fluorometric resazurin-based cell viability assay (in vitro toxicology assay kit; Sigma-Aldrich, Taufkirchen, Germany). Colon (HT-29 and Colo320), prostate (PC-3), breast cancer cell lines (MDA-MB-468 and MDA-MB-231), the chemically transformed but normal mammary gland epithelium cell line 184B5, as well as the S10 Ewing`s sarcoma family cell line SK-N-MC were seeded with low densities into 96- well plates (4,000 - 20,000 cells per well; seeding confluency &tide; 10 - 20%), and were allowed to adhere for 24 h. Subsequently, the compounds and peptide-toxin conjugate 8 - diluted to appropriate concentrations in the respective culture medium - were added to the cells. HT-29, Colo320 and PC-3 cells were treated for 72 h with tubulysin A, 2, 8 and 9. SK-N-MC, MDA-MB-468, MDA-MB-231 and 184B5 cells were initially incubated with the peptide-toxin conjugate 8 for 6 h. After that initial incubation, the incubation solution was discarded, the cells were rinsed once with cell culture medium, and subsequently were allowed to proliferate in compound-free medium until 72 h were reached. Alternatively, SK-N-MC, MDA-MB-468, MDA-MB231 and 184B5 cells were incubated for the whole experimental period of 72 h with the test items. Finally, resazurin solution in DMEM was added to yield a final resazurin concentration of 50 &mu;M, and cells were incubated under standard growth conditions for 2 h. The conversion of resazurin to resorufin by viable, metabolically active cells was measured using a Synergy 2 multiwell plate reader (BioTek, Bad Friedrichshall, Germany) with 540 nm excitation and 590 nm emission filter setting. Non-linear regression analyses of these data was done by using GraphPad Prism software to calculate IC50 values."	PC-3 cell	REF00056
PEP00159	"[K4(C-&beta;A-),F7,L17,P34]-hNPY"	IC50	0.14 &plusmn; 0.02 nM	"Antiproliferative and cytotoxic effects, respectively, of the compounds were detected by using a fluorometric resazurin-based cell viability assay (in vitro toxicology assay kit; Sigma-Aldrich, Taufkirchen, Germany). Colon (HT-29 and Colo320), prostate (PC-3), breast cancer cell lines (MDA-MB-468 and MDA-MB-231), the chemically transformed but normal mammary gland epithelium cell line 184B5, as well as the S10 Ewing`s sarcoma family cell line SK-N-MC were seeded with low densities into 96- well plates (4,000 - 20,000 cells per well; seeding confluency &tide; 10 - 20%), and were allowed to adhere for 24 h. Subsequently, the compounds and peptide-toxin conjugate 8 - diluted to appropriate concentrations in the respective culture medium - were added to the cells. HT-29, Colo320 and PC-3 cells were treated for 72 h with tubulysin A, 2, 8 and 9. SK-N-MC, MDA-MB-468, MDA-MB-231 and 184B5 cells were initially incubated with the peptide-toxin conjugate 8 for 6 h. After that initial incubation, the incubation solution was discarded, the cells were rinsed once with cell culture medium, and subsequently were allowed to proliferate in compound-free medium until 72 h were reached. Alternatively, SK-N-MC, MDA-MB-468, MDA-MB231 and 184B5 cells were incubated for the whole experimental period of 72 h with the test items. Finally, resazurin solution in DMEM was added to yield a final resazurin concentration of 50 &mu;M, and cells were incubated under standard growth conditions for 2 h. The conversion of resazurin to resorufin by viable, metabolically active cells was measured using a Synergy 2 multiwell plate reader (BioTek, Bad Friedrichshall, Germany) with 540 nm excitation and 590 nm emission filter setting. Non-linear regression analyses of these data was done by using GraphPad Prism software to calculate IC50 values."	HT-29 cell	REF00056
PEP00159	"[K4(C-&beta;A-),F7,L17,P34]-hNPY"	IC50	0.46 &plusmn; 0.05 nM	"Antiproliferative and cytotoxic effects, respectively, of the compounds were detected by using a fluorometric resazurin-based cell viability assay (in vitro toxicology assay kit; Sigma-Aldrich, Taufkirchen, Germany). Colon (HT-29 and Colo320), prostate (PC-3), breast cancer cell lines (MDA-MB-468 and MDA-MB-231), the chemically transformed but normal mammary gland epithelium cell line 184B5, as well as the S10 Ewing`s sarcoma family cell line SK-N-MC were seeded with low densities into 96- well plates (4,000 - 20,000 cells per well; seeding confluency &tide; 10 - 20%), and were allowed to adhere for 24 h. Subsequently, the compounds and peptide-toxin conjugate 8 - diluted to appropriate concentrations in the respective culture medium - were added to the cells. HT-29, Colo320 and PC-3 cells were treated for 72 h with tubulysin A, 2, 8 and 9. SK-N-MC, MDA-MB-468, MDA-MB-231 and 184B5 cells were initially incubated with the peptide-toxin conjugate 8 for 6 h. After that initial incubation, the incubation solution was discarded, the cells were rinsed once with cell culture medium, and subsequently were allowed to proliferate in compound-free medium until 72 h were reached. Alternatively, SK-N-MC, MDA-MB-468, MDA-MB231 and 184B5 cells were incubated for the whole experimental period of 72 h with the test items. Finally, resazurin solution in DMEM was added to yield a final resazurin concentration of 50 &mu;M, and cells were incubated under standard growth conditions for 2 h. The conversion of resazurin to resorufin by viable, metabolically active cells was measured using a Synergy 2 multiwell plate reader (BioTek, Bad Friedrichshall, Germany) with 540 nm excitation and 590 nm emission filter setting. Non-linear regression analyses of these data was done by using GraphPad Prism software to calculate IC50 values."	Colo320 cell	REF00056
PEP00029	GnRH analogs 2	Cell viability	39%	"The antiproliferative effects of Dox and GnRH-Dox conjugates were determined in MCF-7 cells using the MTT assay.The results of antiproliferative activity of the three conjugates demonstrated that [d-Cys6-des-Gly10-Pro9-NHEt]-GnRH might have higher binding affinity to GnRH receptors than that of [d-Cys6, desGly10, Pro9-NH2]-GnRH and [d-Cys6, a-aza-Gly10-NH2]-GnRH."	MCF-7 cell; 75 &mu;M	REF00049
PEP00027	GnRH analogs 3	Cell viability	35%	"The antiproliferative effects of Dox and GnRH-Dox conjugates were determined in MCF-7 cells using the MTT assay.The results of antiproliferative activity of the three conjugates demonstrated that [d-Cys6-des-Gly10-Pro9-NHEt]-GnRH might have higher binding affinity to GnRH receptors than that of [d-Cys6, desGly10, Pro9-NH2]-GnRH and [d-Cys6, a-aza-Gly10-NH2]-GnRH."	MCF-7 cell; 75 &mu;M	REF00049
PEP00028	GnRH analogs 1	Cell viability	29%	"The antiproliferative effects of Dox and GnRH-Dox conjugates were determined in MCF-7 cells using the MTT assay.The results of antiproliferative activity of the three conjugates demonstrated that [d-Cys6-des-Gly10-Pro9-NHEt]-GnRH might have higher binding affinity to GnRH receptors than that of [d-Cys6, desGly10, Pro9-NH2]-GnRH and [d-Cys6, a-aza-Gly10-NH2]-GnRH."	MCF-7 cell; 75 &mu;M	REF00049
PEP00029	GnRH analogs 2	Cell viability	50%	"The antiproliferative effects of Dox and GnRH-Dox conjugates were determined in MCF-7 cells using the MTT assay.The results of antiproliferative activity of the three conjugates demonstrated that [d-Cys6-des-Gly10-Pro9-NHEt]-GnRH might have higher binding affinity to GnRH receptors than that of [d-Cys6, desGly10, Pro9-NH2]-GnRH and [d-Cys6, a-aza-Gly10-NH2]-GnRH."	MCF-7 cell; 50 &mu;M	REF00049
PEP00027	GnRH analogs 3	Cell viability	48%	"The antiproliferative effects of Dox and GnRH-Dox conjugates were determined in MCF-7 cells using the MTT assay.The results of antiproliferative activity of the three conjugates demonstrated that [d-Cys6-des-Gly10-Pro9-NHEt]-GnRH might have higher binding affinity to GnRH receptors than that of [d-Cys6, desGly10, Pro9-NH2]-GnRH and [d-Cys6, a-aza-Gly10-NH2]-GnRH."	MCF-7 cell; 50 &mu;M	REF00049
PEP00028	GnRH analogs 1	Cell viability	43%	"The antiproliferative effects of Dox and GnRH-Dox conjugates were determined in MCF-7 cells using the MTT assay.The results of antiproliferative activity of the three conjugates demonstrated that [d-Cys6-des-Gly10-Pro9-NHEt]-GnRH might have higher binding affinity to GnRH receptors than that of [d-Cys6, desGly10, Pro9-NH2]-GnRH and [d-Cys6, a-aza-Gly10-NH2]-GnRH."	MCF-7 cell; 50 &mu;M	REF00049
PEP00029	GnRH analogs 2	Cell viability	59%	"The antiproliferative effects of Dox and GnRH-Dox conjugates were determined in MCF-7 cells using the MTT assay.The results of antiproliferative activity of the three conjugates demonstrated that [d-Cys6-des-Gly10-Pro9-NHEt]-GnRH might have higher binding affinity to GnRH receptors than that of [d-Cys6, desGly10, Pro9-NH2]-GnRH and [d-Cys6, a-aza-Gly10-NH2]-GnRH."	MCF-7 cell; 25 &mu;M	REF00049
PEP00027	GnRH analogs 3	Cell viability	56%	"The antiproliferative effects of Dox and GnRH-Dox conjugates were determined in MCF-7 cells using the MTT assay.The results of antiproliferative activity of the three conjugates demonstrated that [d-Cys6-des-Gly10-Pro9-NHEt]-GnRH might have higher binding affinity to GnRH receptors than that of [d-Cys6, desGly10, Pro9-NH2]-GnRH and [d-Cys6, a-aza-Gly10-NH2]-GnRH."	MCF-7 cell; 25 &mu;M	REF00049
PEP00028	GnRH analogs 1	Cell viability	52%	"The antiproliferative effects of Dox and GnRH-Dox conjugates were determined in MCF-7 cells using the MTT assay.The results of antiproliferative activity of the three conjugates demonstrated that [d-Cys6-des-Gly10-Pro9-NHEt]-GnRH might have higher binding affinity to GnRH receptors than that of [d-Cys6, desGly10, Pro9-NH2]-GnRH and [d-Cys6, a-aza-Gly10-NH2]-GnRH."	MCF-7 cell; 25 &mu;M	REF00049
PEP00029	GnRH analogs 2	Cell viability	30%	"The antiproliferative effects of Dox and GnRH-Dox conjugates were determined in MCF-7 cells using the MTT assay.The results of antiproliferative activity of the three conjugates demonstrated that [d-Cys6-des-Gly10-Pro9-NHEt]-GnRH might have higher binding affinity to GnRH receptors than that of [d-Cys6, desGly10, Pro9-NH2]-GnRH and [d-Cys6, a-aza-Gly10-NH2]-GnRH."	MCF-7 cell; 100 &mu;M	REF00049
PEP00027	GnRH analogs 3	Cell viability	26%	"The antiproliferative effects of Dox and GnRH-Dox conjugates were determined in MCF-7 cells using the MTT assay.The results of antiproliferative activity of the three conjugates demonstrated that [d-Cys6-des-Gly10-Pro9-NHEt]-GnRH might have higher binding affinity to GnRH receptors than that of [d-Cys6, desGly10, Pro9-NH2]-GnRH and [d-Cys6, a-aza-Gly10-NH2]-GnRH."	MCF-7 cell; 100 &mu;M	REF00049
PEP00028	GnRH analogs 1	Cell viability	15%	"The antiproliferative effects of Dox and GnRH-Dox conjugates were determined in MCF-7 cells using the MTT assay.The results of antiproliferative activity of the three conjugates demonstrated that [d-Cys6-des-Gly10-Pro9-NHEt]-GnRH might have higher binding affinity to GnRH receptors than that of [d-Cys6, desGly10, Pro9-NH2]-GnRH and [d-Cys6, a-aza-Gly10-NH2]-GnRH."	MCF-7 cell; 100 &mu;M	REF00049
PEP00167	DT7	K<sub>D</sub>	22&plusmn;1 nM	"Recombinant anti-transferrin receptor antibody was captured by the Protein A sensor chip at the concentration of 15 &mu;g/mL with a level of &tide;6000 response units (RU) [28]. Then, the DT7 peptide was dissolved in HBS-EP buffer at a series of defined concentrations (78, 156, 313, and 1250 nM) and injected for recording resonance changes to assess the binding affinity."	Protein A sensor chip in the vitro	REF003351
PEP00076	P-(A5G27)-FITC	Percentage of labeled cells	98%	"4T1-Luc and B16-F10 cells were collected after trypsinization of cell monolayers. Cells (5 10<sup>5</sup>) were incubated in 3% BSA for 30 min at room temperature and then treated with 50 &mu;g/mL of the FITC-labeled P-(A5G27) or P-(A5G27scrm) in 0.5 mL of PBS containing 1% BSA for 1 h at 4 &deg;C or for 4 h at 37 &deg;C. Cells were then washed twice with PBS, and the fluorescence intensity was analyzed by Guava easyCyte flow cytometer (EMD Millipore, excitation at 488 nm and emission at 525 nm)."	4T1-Luc and B16-F10 cells	REF00041
PEP00078	P-(A5G27scrm)-FITC	Percentage of labeled cells	62%	"4T1-Luc and B16-F10 cells were collected after trypsinization of cell monolayers. Cells (5 10<sup>5</sup>) were incubated in 3% BSA for 30 min at room temperature and then treated with 50 &mu;g/mL of the FITC-labeled P-(A5G27) or P-(A5G27scrm) in 0.5 mL of PBS containing 1% BSA for 1 h at 4 &deg;C or for 4 h at 37 &deg;C. Cells were then washed twice with PBS, and the fluorescence intensity was analyzed by Guava easyCyte flow cytometer (EMD Millipore, excitation at 488 nm and emission at 525 nm)."	4T1-Luc and B16-F10 cells	REF00041
PEP00060	p4	Binding rate	2.17%	"To assess the binding capacity of the candidate peptides, peptide-FITC conjugates were incubated at 0, 4 or 8 ?M with 10<sup>6</sup> PBMC cells at 37 C for 30 min."	Mouse peripheral mononuclear cell PBMC	REF00036
PEP00099	p6	Binding rate	2.17%	"To assess the binding capacity of the candidate peptides, peptide-FITC conjugates were incubated at 0, 4 or 8 ?M with 10<sup>6</sup> PBMC cells at 37 C for 30 min."	Mouse peripheral mononuclear cell PBMC	REF00036
PEP00060	p4	Binding rate	10.30%	"To assess the binding capacity of the candidate peptides, peptide-FITC conjugates were incubated at 0, 4 or 8 ?M with 10<sup>6</sup> NB4 cells at 37 C for 30 min."	Human leukemic cell NB4	REF00036
PEP00060	p4	Binding rate	0.82%	"To assess the binding capacity of the candidate peptides, peptide-FITC conjugates were incubated at 0, 4 or 8 ?M with 10<sup>6</sup> MOPC 315.BM cells at 37 C for 30 min."	MOPC 315.BM cell	REF00036
PEP00060	p4	Binding rate	13.80%	"To assess the binding capacity of the candidate peptides, peptide-FITC conjugates were incubated at 0, 4 or 8 ?M with 10<sup>6</sup> HL-60 cells at 37 C for 30 min."	Human leukemic cell HL-60	REF00036
PEP00099	p6	Binding rate	6.90%	"To assess the binding capacity of the candidate peptides, peptide-FITC conjugates were incubated at 0, 4 or 8 ?M with 10<sup>6</sup> HL-60 cells at 37 C for 30 min."	Human leukemic cell HL-60	REF00036
PEP00060	p4	Binding rate	80.90%	"To assess the binding capacity of the candidate peptides, peptide-FITC conjugates were incubated at 0, 4 or 8 ?M with 10<sup>6</sup> A20 cells at 37 C for 30 min."	A20 cell	REF00036
PEP00160	123B9	Binding constant	3.9 &mu;M	"To further verify the binding affinity and selectivity of the resulting conjugates for the EphA2 ligand-binding domain (LBD), we expressed and purified the EphA2 and EphA4 ligand-binding domains (EphA2-LBD and EphA4-LBD). These proteins were dissolved to final concentrations of 100 &mu;M in 50 mM phosphate buffer (pH = 6.5) containing 100 mM NaCl. The isothermal-titration-calorimetry (ITC) measurements under these experimental conditions revealed that 123B9 and the (123B9)2-motif bound to EphA2 with similarKdvalues of 3.9 and 4.9 &mu;M, respectively (Figure"	.	REF00035
PEP00095	ABD-RPARPAR	A<sub>280nm</sub>	320 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Transferrin(ABD-RPARPAR: Tf 1: 5)	REF00030
PEP00095	ABD-RPARPAR	A<sub>280nm</sub>	140 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Transferrin(ABD-RPARPAR: Tf 1: 2)	REF00030
PEP00095	ABD-RPARPAR	A<sub>280nm</sub>	700 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Transferrin(ABD-RPARPAR: Tf 1: 10)	REF00030
PEP00095	ABD-RPARPAR	A<sub>280nm</sub>	70 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Transferrin(ABD-RPARPAR: Tf 1: 1)	REF00030
PEP00095	ABD-RPARPAR	A<sub>280nm</sub>	0 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Transferrin(ABD-RPARPAR: Tf 1: 0)	REF00030
PEP00094	ABD-RGDK	A<sub>280nm</sub>	440 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Transferrin(ABD-RGDK: Tf 1: 5)	REF00030
PEP00094	ABD-RGDK	A<sub>280nm</sub>	170 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Transferrin(ABD-RGDK: Tf 1: 2)	REF00030
PEP00094	ABD-RGDK	A<sub>280nm</sub>	800 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Transferrin(ABD-RGDK: Tf 1: 10)	REF00030
PEP00094	ABD-RGDK	A<sub>280nm</sub>	75 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Transferrin(ABD-RGDK: Tf 1: 1)	REF00030
PEP00094	ABD-RGDK	A<sub>280nm</sub>	0 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Transferrin(ABD-RGDK: Tf 1: 0)	REF00030
PEP00095	ABD-RPARPAR	A<sub>280nm</sub>	280 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Human serum albumin(ABD-RPARPAR: HSA 1: 5)	REF00030
PEP00095	ABD-RPARPAR	A<sub>280nm</sub>	130 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Human serum albumin(ABD-RPARPAR: HSA 1: 2)	REF00030
PEP00095	ABD-RPARPAR	A<sub>280nm</sub>	520 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Human serum albumin(ABD-RPARPAR: HSA 1: 10)	REF00030
PEP00095	ABD-RPARPAR	A<sub>280nm</sub>	70 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Human serum albumin(ABD-RPARPAR: HSA 1: 1)	REF00030
PEP00095	ABD-RPARPAR	A<sub>280nm</sub>	0 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Human serum albumin(ABD-RPARPAR: HSA 1: 0)	REF00030
PEP00094	ABD-RGDK	A<sub>280nm</sub>	230 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Human serum albumin(ABD-RGDK: HSA 1: 5)	REF00030
PEP00094	ABD-RGDK	A<sub>280nm</sub>	80 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Human serum albumin(ABD-RGDK: HSA 1: 2)	REF00030
PEP00094	ABD-RGDK	A<sub>280nm</sub>	670 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Human serum albumin(ABD-RGDK: HSA 1: 10)	REF00030
PEP00094	ABD-RGDK	A<sub>280nm</sub>	75 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Human serum albumin(ABD-RGDK: HSA 1: 1)	REF00030
PEP00094	ABD-RGDK	A<sub>280nm</sub>	0 mAU	"To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 &mu;L of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA."	Human serum albumin(ABD-RGDK: HSA 1: 0)	REF00030
PEP00161	Peptide 18-4	K<sub>D</sub>	0.98 &mu;M	"A series of SPR experiments were carried out at various concentrations of KRT1 fragment protein (0.1, 1, 10, 100 &mu;M) ."	KRT1 fragment protein	REF003341
PEP00097	A20FMDV2	IC50	45 &plusmn; 4.1 nM	The activity and selectivity of integrin ligands were determined by a solid-phase binding assay using coated extracellular matrix proteins and soluble integrins.	LAP (TGF-&beta;)(&alpha;v&beta;6)	REF003331
PEP00124	c(RGDyK)	IC50	&gt; 10000 nM	The activity and selectivity of integrin ligands were determined by a solid-phase binding assay using coated extracellular matrix proteins and soluble integrins.	LAP (TGF-&beta;)(&alpha;v&beta;6)	REF003331
PEP00124	c(RGDyK)	IC50	236 &plusmn; 45 nM	The activity and selectivity of integrin ligands were determined by a solid-phase binding assay using coated extracellular matrix proteins and soluble integrins.	LAP (TGF-b)(&alpha;v&beta;8)	REF003331
PEP00097	A20FMDV2	IC50	&gt; 10000 nM	The activity and selectivity of integrin ligands were determined by a solid-phase binding assay using coated extracellular matrix proteins and soluble integrins.	LAP (TGF-b)(&alpha;v&beta;8)	REF003331
PEP00124	c(RGDyK)	IC50	86 &plusmn; 7 nM	The activity and selectivity of integrin ligands were determined by a solid-phase binding assay using coated extracellular matrix proteins and soluble integrins.	Human vitronectin(&alpha;v&beta;5)	REF003331
PEP00097	A20FMDV2	IC50	0.93 &plusmn; 0.07 nM	The activity and selectivity of integrin ligands were determined by a solid-phase binding assay using coated extracellular matrix proteins and soluble integrins.	Human vitronectin(&alpha;v&beta;5)	REF003331
PEP00124	c(RGDyK)	IC50	3.8 &plusmn; 0.42 nM	The activity and selectivity of integrin ligands were determined by a solid-phase binding assay using coated extracellular matrix proteins and soluble integrins.	Human vitronectin(&alpha;v&beta;3)	REF003331
PEP00097	A20FMDV2	IC50	&gt; 10000 nM	The activity and selectivity of integrin ligands were determined by a solid-phase binding assay using coated extracellular matrix proteins and soluble integrins.	Human vitronectin(&alpha;v&beta;3)	REF003331
PEP00124	c(RGDyK)	IC50	503 &plusmn; 55 nM	The activity and selectivity of integrin ligands were determined by a solid-phase binding assay using coated extracellular matrix proteins and soluble integrins.	Human fibronectin(&alpha;5&beta;1)	REF003331
PEP00097	A20FMDV2	IC50	&gt; 10000 nM	The activity and selectivity of integrin ligands were determined by a solid-phase binding assay using coated extracellular matrix proteins and soluble integrins.	Human fibronectin(&alpha;5&beta;1)	REF003331
PEP00097	A20FMDV2	IC50	&gt; 10000 nM	The activity and selectivity of integrin ligands were determined by a solid-phase binding assay using coated extracellular matrix proteins and soluble integrins.	Human fibrinogen(&alpha;IIb&beta;3)	REF003331
PEP00124	c(RGDyK)	IC50	&gt; 10000 nM	The activity and selectivity of integrin ligands were determined by a solid-phase binding assay using coated extracellular matrix proteins and soluble integrins.	Human fibrinogen(&alpha;IIb&beta;3)	REF003331
PEP00040	EETI-2.5Z	IC50	1.1 &plusmn; 0.2 nM	.	U87MG cell	REF00012
PEP00158	"[K4,F7,K22,P34]-NPY"	EC50	7.1&plusmn;0.1 nM	"Signal transduction inositol phosphate (IP) accumulation assay was performed like described before.(40)Briefly, stably transfected COS-7 cells were seeded into 48-well plates (50000 cells per well) and cultured overnight. After labeling cells with 2 &mu;Ci/mL myo-[2-3H]-inositol in culture medium without penicillin and streptomycin, cells were washed and incubated with peptide concentrations ranging from 10<sup>-5</sup>to 10<sup>-12</sup>M in DMEM supplied with 10 mM LiCl for 1 h at 37 &deg;C. Radioactive IP species were isolated by anion exchange chromatography and measured in a scintillation counter. EC50and pEC50values were calculated from concentration-response curves by using nonlinear regression (GraphPad Prism 5.0). Assays were performed in duplicate in at least two independent experiments."	COS-7 cells; hY<sub>2</sup>R	REF00009
PEP00158	"[K4,F7,K22,P34]-NPY"	EC50	87 nM	"Signal transduction inositol phosphate (IP) accumulation assay was performed like described before.(40)Briefly, stably transfected COS-7 cells were seeded into 48-well plates (50000 cells per well) and cultured overnight. After labeling cells with 2 &mu;Ci/mL myo-[2-3H]-inositol in culture medium without penicillin and streptomycin, cells were washed and incubated with peptide concentrations ranging from 10<sup>-5</sup>to 10<sup>-12</sup>M in DMEM supplied with 10 mM LiCl for 1 h at 37 &deg;C. Radioactive IP species were isolated by anion exchange chromatography and measured in a scintillation counter. EC50and pEC50values were calculated from concentration-response curves by using nonlinear regression (GraphPad Prism 5.0). Assays were performed in duplicate in at least two independent experiments."	COS-7 cells; hY<sub>2</sup>R	REF00009
PEP00158	"[K4,F7,K22,P34]-NPY"	EC50	8.3&plusmn;0.1 nM	"Signal transduction inositol phosphate (IP) accumulation assay was performed like described before.(40)Briefly, stably transfected COS-7 cells were seeded into 48-well plates (50000 cells per well) and cultured overnight. After labeling cells with 2 &mu;Ci/mL myo-[2-3H]-inositol in culture medium without penicillin and streptomycin, cells were washed and incubated with peptide concentrations ranging from 10<sup>-5</sup>to 10<sup>-12</sup>M in DMEM supplied with 10 mM LiCl for 1 h at 37 &deg;C. Radioactive IP species were isolated by anion exchange chromatography and measured in a scintillation counter. EC50and pEC50values were calculated from concentration-response curves by using nonlinear regression (GraphPad Prism 5.0). Assays were performed in duplicate in at least two independent experiments."	COS-7 cells; hY<sub>1</sup>R	REF00009
PEP00158	"[K4,F7,K22,P34]-NPY"	EC50	5 nM	"Signal transduction inositol phosphate (IP) accumulation assay was performed like described before.(40)Briefly, stably transfected COS-7 cells were seeded into 48-well plates (50000 cells per well) and cultured overnight. After labeling cells with 2 &mu;Ci/mL myo-[2-3H]-inositol in culture medium without penicillin and streptomycin, cells were washed and incubated with peptide concentrations ranging from 10<sup>-5</sup>to 10<sup>-12</sup>M in DMEM supplied with 10 mM LiCl for 1 h at 37 &deg;C. Radioactive IP species were isolated by anion exchange chromatography and measured in a scintillation counter. EC50and pEC50values were calculated from concentration-response curves by using nonlinear regression (GraphPad Prism 5.0). Assays were performed in duplicate in at least two independent experiments."	COS-7 cells; hY<sub>1</sup>R	REF00009
PEP00081	Heptapeptide	K<sub>D</sub>	65.3 &mu;M	"One flow cell of CM5 sensor chip was activated with a 1:1 mixture of 0.2 M EDC and 0.05 M NHS in water as described by the manufacturer. Hsp90 of 50 &mu;g/ml was injected over the flow cell for 5 min in 10 mM sodium acetate, pH 4.5 at a flow rate of 10 &mu;l/min. The remaining binding sites were blocked by 1 M ethanolamine, pH 8.5. 7200 RU of Hsp90 was immobilized.Peptides with different concentrations were injected over the Hsp90 surface and blank flow cell for 1 min at a flow rate of 30 &mu;l/min. No specific binding to a blank flow cell was subtracted to obtain the corrected sensorgrams. Data were analyzed with the BIAcore T100 evaluation software by fitting to steady state affinity model."	CM5 sensor chip in the vitro	REF003311