Peptide name : Pep

Source/Organism : Synthetic

Linear/Cyclic : Linear

Chirality : L

Peptide length: 21

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information:

Assay type : MTT assay

Assay time : 24-h

Activity : IC50 = 4 µM

Cell line : A-549

Cancer type : Lung Cancer

Other activity : Antimicrobial and Anticancer

Amino acid composition bar chart :

Molecular mass : 2623.3233 Dalton

Aliphatic index : 0.928

Instability index : 10.219

Hydrophobicity (GRAVY) : -1.009

Isoelectric point : 11.535

Charge (pH 7) : 9.7511

Aromaticity : 14.28

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

Hydrophobic/hydrophilic ratio : 1.1

hydrophobic moment : -0.459

Missing amino acid : C,D,E,F,H,M,N,P,Q,S,T,Y

Most occurring amino acid : K

Most occurring amino acid frequency : 9

Least occurring amino acid : R

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (61., 9.5, 38.)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)CN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)O)C(C)C

1 : Thankappan B, et al. Dual antimicrobial and anticancer activity of a novel synthetic α-helical antimicrobial peptide. Eur J Pharm Sci. 2021; 161:105784. doi: 10.1016/j.ejps.2021.105784

Paper title : Dual antimicrobial and anticancer activity of a novel synthetic α-helical antimicrobial peptide.

Doi : https://doi.org/10.1016/j.ejps.2021.105784

Abstract : Antimicrobial peptides (AMPs) are increasingly sought-after and researched antimicrobial agents due to its desired pharmacological properties and the continuous diminishing efficacy of antibiotics. In addition to this line of research, the aim of the present study is to determine the antimicrobial and anticancer activity of a de novo designed α-helical peptide. Circular dichroism showed 100% helical nature of the peptide in 10 mM SDS. Notably, the peptide exerted significant antimicrobial activity against the reference and antibiotic-resistant clinical isolates belonging to Pseudomonas sp. at a MIC and MBC of 2 and 8 μM, respectively. The progressive disruption and disturbance of cell membrane in the overall topography was observed in the scanning electron microscopy (SEM) micrographs of Pseudomonas aeruginosa ATCC 27853 treated with the peptide as compared to untreated control. The results of time-kill kinetics showed complete lysis at 3x MIC after 50 min of incubation of the microbe with the peptide. Moreover, the peptide did not lyse human RBCs even at the highest concentration of the peptide (10 mM) and retained its activity upon treatment at 0.5 mg/ml trypsin. Cancer cell lines, viz. A549 and MCF-7 were also found to be sensitive to peptide activity showing 50% reduction in survivability at 4 and 2 μM, respectively; however, L929 cells were unaffected. Drastic membrane permeability and necrotic mode of lysis of peptide-treated-A549 cells were affirmed by propidium iodide and live/dead cell staining. The results showed that the designed peptide could be an efficient drug molecule for clinical studies subjected to successful experiments on animal models.