Peptide name : Ponericin-W1 (11-25) [P4K

Source/Organism : Synthetic

Linear/Cyclic : Linear

Chirality : L

Peptide length: 15

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information:

Assay type : MTT assay

Assay time : Not Available

Activity : IC50 = 4.3 µM

Cell line : A-549

Cancer type : Lung Cancer

Other activity : Antimicrobial

Amino acid composition bar chart :

Molecular mass : 1826.4452 Dalton

Aliphatic index : 1.686

Instability index : -36.566

Hydrophobicity (GRAVY) : 0.1933

Isoelectric point : 10.778

Charge (pH 7) : 6.7531

Aromaticity : 6.666

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

Hydrophobic/hydrophilic ratio : 1.1429

hydrophobic moment : -2.422

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

Most occurring amino acid : K

Most occurring amino acid frequency : 7

Least occurring amino acid : F

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (80, 0, 53.)

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

1 : Pan F, et al. Anticancer effect of rationally designed α-helical amphiphilic peptides. Colloids Surf B Biointerfaces. 2022; 220:112841. doi: 10.1016/j.colsurfb.2022.112841

Paper title : Anticancer effect of rationally designed α-helical amphiphilic peptides.

Doi : https://doi.org/10.1016/j.colsurfb.2022.112841

Abstract : Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications.