Peptide name : ES-2

Source/Organism : Endostatin derived synthetic peptide

Linear/Cyclic : Linear

Chirality : L

Peptide length: 11

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : Not found

Activity : 60% inhibition at 2.5µg/ml

Cell line : BAE

Cancer type : Tumor

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 1223.4283 Dalton

Aliphatic index : 1.154

Instability index : 56.3818

Hydrophobicity (GRAVY) : -0.027

Isoelectric point : 11.699

Charge (pH 7) : 1.7612

Aromaticity : 0

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : 1.75

hydrophobic moment : 0.8714

Missing amino acid : C,W,H,Q,T,M,E,K,S,F,Y,L,N,G

Most occurring amino acid : R

Most occurring amino acid frequency : 3

Least occurring amino acid : I

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.1, 0.2)

SMILES Notation: CC[C@H](C)[C@H](N)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)N1CCC[C@H]1C(=O)O)C(C)C)C(C)C

1 : Yin R, et al. Effect of RGD-4C position is more important than disulfide bonds on antiangiogenic activity of RGD-4C modified endostatin derived synthetic polypeptide. Bioconjug Chem. 2010; 21:1142-7. doi: 10.1021/bc900292y

Paper title : Effect of RGD-4C position is more important than disulfide bonds on antiangiogenic activity of RGD-4C modified endostatin derived synthetic polypeptide.

Doi : https://doi.org/10.1021/bc900292y

Abstract : ES-2 (IVRRADRAAVP), an endostatin-derived synthetic polypeptide, contains the amino acids 50-60 of endostatin from its N terminus, and it had no inhibitory effects on tumor growth in vivo. In order to increase the targeted delivery of ES-2 to tumors and further enhance the activity, the polypeptide RGD-4C (ACDCRGDCFC) was introduced into ES-2, and the effects of RGD-4C position and RGD-4C disulfide bonds on polypeptides activity were investigated. When RGD-4C polypeptides (with or without disulfide bonds) were introduced to the N-terminals of synthesized ES-2, the modified ES-2 showed significant antitumor activity in vivo. Cell proliferation and chicken chorioallantoic membrane (CAM) assay results showed that disulfide bonds had no significant effects on RGD-4C-modified ES-2 antiangiogenic activity. Furthermore, the target of modified peptides was integrin alpha5beta1, rather than integrin alphavbeta3 as previous studies mentioned.