Peptide name : hP3

Source/Organism : Human endostatin peptides

Linear/Cyclic : Linear

Chirality : L

Peptide length: 25

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: None

Assay type : Matrigel assay

Assay time : 72h

Activity : No inhibition at 7 mg/kg/d

Cell line : BxPC-3

Cancer type : Pancreatic cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2912.3084 Dalton

Aliphatic index : 1.016

Instability index : 63.792

Hydrophobicity (GRAVY) : -0.012

Isoelectric point : 11.417

Charge (pH 7) : 2.3994

Aromaticity : 0.12

Molar extinction coefficient (cysteine, cystine): (1490, 1490)

Hydrophobic/hydrophilic ratio : 0.92307692

hydrophobic moment : -0.558

Missing amino acid : C,W,H,P,M,E,K,N,G

Most occurring amino acid : R

Most occurring amino acid frequency : 5

Least occurring amino acid : T

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.2, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CO)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](N)[C@@H](C)O)C(=O)N[C@H](C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)O)C(C)C)C(C)C

1 : Tjin Tham Sjin RM, et al. A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity. Cancer Res. 2005; 65:3656-63. doi: 10.1158/0008-5472.CAN-04-1833

Paper title : A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity.

Doi : https://doi.org/10.1158/0008-5472.CAN-04-1833

Abstract : The first recombinant endostatin that elicited strong antitumor activity was expressed in Escherichia coli and administered as a suspension. Under these conditions, the protein retained its full antiangiogenic activity. Lack of requirement for a folded structure prompted us to investigate antitumor properties of synthetic peptides corresponding to different regions of endostatin. Here, we show that the entire antitumor, antimigration, and antipermeability activities of endostatin are mimicked by a 27-amino-acid peptide corresponding to the NH2-terminal domain of endostatin. This peptide contains three histidines that are responsible for zinc binding. Mutations of the zinc-binding histidines abolished its antitumor and antimigration activities, but not antipermeability properties.