Peptide name : ChMAP-28

Source/Organism : Domestic goat

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 27

C-terminal modification: Not found

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : Cytotoxic Activity assay, Lactate dehydrogenase (LDH)-Releaseassay, MTT assay

Assay time : 48h

Activity : IC50 : 3.39 ± 0.15 μM

Cell line : HL-60

Cancer type : Acute promyelocytic leukemia

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 3365.0794 Dalton

Aliphatic index : 0.792

Instability index : 69.3407

Hydrophobicity (GRAVY) : -0.659

Isoelectric point : 12

Charge (pH 7) : 8.9284

Aromaticity : 0.185

Molar extinction coefficient (cysteine, cystine): (6990, 6990)

Hydrophobic/hydrophilic ratio : 1.25

hydrophobic moment : -1.708

Missing amino acid : C,Q,T,M,E,S,D,N,A

Most occurring amino acid : K

Most occurring amino acid frequency : 5

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.1, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CCCNC(=N)N)NC(=O)CN)C(C)C)C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)O

1 : Emelianova AA, et al. Anticancer Activity of the Goat Antimicrobial Peptide ChMAP-28. Front Pharmacol. 2018; 9:1501. doi: 10.3389/fphar.2018.01501

Paper title : Anticancer Activity of the Goat Antimicrobial Peptide ChMAP-28.

Doi : https://doi.org/10.3389/fphar.2018.01501

Abstract : Cytotoxic effect of the antimicrobial peptide ChMAP-28 from leucocytes of the goat Capra hircus was examined against five cancer and two normal human cell lines. ChMAP-28 has the amino acid sequence GRFKRFRKKLKRLWHKVGPFVGPILHY and is homologous to other α-helical mammalian antimicrobial peptides. ChMAP-28 shows considerably higher cytotoxicity against cultured tumor cells than toward normal cells at concentrations of <10 μM. Our findings suggest that ChMAP-28 can initiate necrotic death of cancer cells. Its cytotoxic effect is accomplished due to disruption of the plasma membrane integrity and is not abrogated by the addition of the caspase inhibitor Z-VAD-FMK. ChMAP-28 causes permeabilization of cytoplasmic membrane of human leukemia cells HL-60 already after 15 min of incubation. Here, we show that ChMAP-28 has one of the highest antitumor activity in vitro among all known antimicrobial peptides. We speculate that the observed specificity of ChMAP-28 cytotoxic effect against tumor cells is due to its relatively low hydrophobicity and high cationicity. In the meantime, this peptide has low hemolytic activity, which generates a potential for its use as a therapeutic agent.