Peptide name : BPC98

Source/Organism : Synthetic Peptide

Linear/Cyclic : Cyclic

Chirality : L

Peptide length: 10

C-terminal modification: Cyclic

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 48h

Activity : IC50 : 40.7 ± 3 μM

Cell line : MDA-MB-231

Cancer type : Cervical cancer

Other activity : Hemolytic activity; Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 1273.6526 Dalton

Aliphatic index : 1.17

Instability index : 9.59

Hydrophobicity (GRAVY) : -0.88

Isoelectric point : 10.602

Charge (pH 7) : 4.7551

Aromaticity : 0.1

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

Hydrophobic/hydrophilic ratio : 0.66666666

hydrophobic moment : 0.2168

Missing amino acid : W,T,P,I,M,E,D,N,G,C,R,H,S,Y,A,V

Most occurring amino acid : K

Most occurring amino acid frequency : 5

Least occurring amino acid : F

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.8, 0, 0.4)

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)O

1 : Feliu L, et al. Antimicrobial cyclic decapeptides with anticancer activity. Peptides. 2010; 31:2017-26. doi: 10.1016/j.peptides.2010.07.027

Paper title : Antimicrobial cyclic decapeptides with anticancer activity.

Doi : https://doi.org/10.1016/j.peptides.2010.07.027

Abstract : Antimicrobial peptides have been considered as potential candidates for cancer therapy. We report here the cytotoxicity of a library of 66 antibacterial cyclodecapeptides on human carcinoma cell lines, and their effects on apoptosis [as assessed by cleavage of poly(ADP-ribose) polymerase (PARP)] and cell signaling proteins (p53 and ERK1/2) in cultured human cervical carcinoma cells. A design of experiments approach permitted to analyze the results of a subset of 16 peptides and define rules for high anticancer activity against MDA-MB-231 breast carcinoma cells. Eight peptides were identified with IC(50) values ranging from 18.5 to 57.5 μM against the five cell lines tested, being HeLa cells the most sensitive. Among these sequences, BPC88, BPC96, BPC98, and BPC194 displayed specificity and high cytotoxicity against HeLa cells (IC(50) of 22.5-38.5 μM), showed low hemolytic activity and low cytotoxicity to non-malignant fibroblasts, and were stable to proteases in human serum. Induction of apoptosis by these peptides was observed and the apoptotic effect of BPC88 and BPC96 caused a marked decrease on the activated form of ERK1/2 kinase and an induction of p53. We further showed that BPC96 at low doses synergized the cytotoxic effect of cisplatin. These findings suggest that cyclic decapeptides may represent novel anticancer agents providing a new strategy in cancer therapy.