Peptide name : Peptide P

Source/Organism : PeptideV13K

Linear/Cyclic : Linear

Chirality : L

Peptide length: 26

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : 36h

Activity : IC50 : 11.5 µMo/L

Cell line : B-16

Cancer type : Skin cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2949.5342 Dalton

Aliphatic index : 0.826

Instability index : 6.5577

Hydrophobicity (GRAVY) : -0.215

Isoelectric point : 10.778

Charge (pH 7) : 6.8403

Aromaticity : 0.115

Molar extinction coefficient (cysteine, cystine): (5500, 5500)

Hydrophobic/hydrophilic ratio : 0.73333333

hydrophobic moment : 0.02

Missing amino acid : C,R,Q,P,M,E,D,Y,N,G

Most occurring amino acid : K

Most occurring amino acid frequency : 7

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.1, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@@H](N)CCCCN)[C@@H](C)O)[C@@H](C)O)C(C)C)[C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)O

1 : Huang YB, et al. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework. Mol Cancer Ther. 2011; 10:416-26. doi: 10.1158/1535-7163.MCT-10-0811

Paper title : Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework.

Doi : https://doi.org/10.1158/1535-7163.MCT-10-0811

Abstract : In the present study, the hydrophobicity of a 26-residue α-helical peptide (peptide P) was altered to study the effects of peptide hydrophobicity on the mechanism of action of cationic anticancer peptides. Hydrophobicity of the nonpolar face of the peptides was shown to correlate with peptide helicity. The self-association ability of peptides in aqueous environment, determined by the reversed-phase high performance liquid chromatography temperature profiling, showed strong influence on anticancer activity. The peptide analogues with greater hydrophobicity showed stronger anticancer activity determined by IC(50) values with a necrotic-like membrane disruption mechanism. Peptide analogues exhibited high specificity against cancer cells and much higher anticancer activity than widely-used anticancer chemical drugs. The mechanism of action of anticancer peptides was also investigated. The hydrophobicity of peptides plays a crucial role in the mechanism of action against cancer cells, which could present a way, using a de novo design approach, to create anticancer peptides as potential therapeutics in clinical practices.