Peptide name : AP1-Z1

Source/Organism : AcrAP1 from the venom of the Arabian scorpion

Linear/Cyclic : Linear

Chirality : L

Peptide length: 18

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information:

Assay type : MTT assay

Assay time : 24-h

Activity : IC50 = 7.222 μM

Cell line : MCF-7

Cancer type : Breast Cancer

Other activity : Antimicrobial

Amino acid composition bar chart :

Molecular mass : 1961.3481 Dalton

Aliphatic index : 1.411

Instability index : -0.5056

Hydrophobicity (GRAVY) : 1.4111

Isoelectric point : 8.7572

Charge (pH 7) : 0.8463

Aromaticity : 16.66

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

Hydrophobic/hydrophilic ratio : 2.6

hydrophobic moment : -0.852

Missing amino acid : C,D,E,M,N,Q,R,T,V,W,Y

Most occurring amino acid : F

Most occurring amino acid frequency : 3

Least occurring amino acid : P

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (33., 27., 50.)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](C)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)Cc1ccccc1)[C@@H](C)CC)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCCCN)C(=O)O)[C@@H](C)CC

1 : Ma R, et al. In Vitro and MD Simulation Study to Explore Physicochemical Parameters for Antibacterial Peptide to Become Potent Anticancer Peptide. Mol Ther Oncolytics. 2020; 16:7-19. doi: 10.1016/j.omto.2019.12.001

Paper title : In Vitro and MD Simulation Study to Explore Physicochemical Parameters for Antibacterial Peptide to Become Potent Anticancer Peptide.

Doi : https://doi.org/10.1016/j.omto.2019.12.001

Abstract : Although the physicochemical properties of antimicrobial peptides (AMPs) and anticancer peptides (ACPs) are very similar, it remains unclear which specific parameter(s) of ACPs confer the major anticancer activity. By answering how to construct a short AMP/ACP that could easily be synthesized in the most cost effective way plus conferring a maximum anticancer effect is a very important scientific breakthrough in the development of protein/peptide drugs. In this study, an 18-amino-acids antimicrobial peptide, AcrAP1 (named AP1-Z1), was used as a template. Bioinformatics algorithms were then performed to design its six mutants (AP1-Z3a, AP1-Z3b, AP1-Z5a, AP1-Z5b, AP1-Z7, and AP1-Z9). After a series of in vitro experiments plus intensive computational analysis, the data demonstrated that AP1-Z5a and AP1-Z5b induced both apoptosis and anti-angiogenic effects to achieve the maximum anticancer activity. Specifically, the most effective mutant, AP1-Z5b, exhibited high selectivity for the charged membrane in molecular dynamics simulations. These findings clearly demonstrated that both charge and hydrophobicity play an important role and are necessary to reach an optimum equilibrium for optimizing the anticancer activity of AMPs. Overall, the present study provides a very crucial theoretical basis and important scientific evidence on the key physicochemical parameters of ACP drugs development.