Peptide name : [Arg]7-VmCT1

Source/Organism : Synthetic

Linear/Cyclic : Linear

Chirality : L

Peptide length: 13

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information:

Assay type : MTT assay

Assay time : 24-h

Activity : IC50 = 18.0 ± 2.7 μmol/L

Cell line : MCF-7

Cancer type : Breast Cancer

Other activity : Antimicrobial and Anticancer

Amino acid composition bar chart :

Molecular mass : 1493.7924 Dalton

Aliphatic index : 1.2

Instability index : 20.9154

Hydrophobicity (GRAVY) : 1.1308

Isoelectric point : 11.000

Charge (pH 7) : 1.7591

Aromaticity : 23.07

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

Hydrophobic/hydrophilic ratio : 3.3333

hydrophobic moment : 1.5257

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

Most occurring amino acid : F

Most occurring amino acid frequency : 2

Least occurring amino acid : G

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (38., 15., 53.)

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

1 : Pedron CN, et al. Net charge tuning modulates the antiplasmodial and anticancer properties of peptides derived from scorpion venom. J Pept Sci. 2021; 27:e3296. doi: 10.1002/psc.3296

Paper title : Net charge tuning modulates the antiplasmodial and anticancer properties of peptides derived from scorpion venom.

Doi : https://doi.org/10.1002/psc.3296

Abstract : VmCT1, a linear helical antimicrobial peptide isolated from the venom of the scorpion Vaejovis mexicanus, displays broad spectrum antimicrobial activity against bacteria, fungi, and protozoa. Analogs derived from this peptide containing single Arg-substitutions have been shown to increase antimicrobial and antiparasitic activities against Trypanossoma cruzi. Here, we tested these analogs against malaria, an infectious disease caused by Plasmodium protozoa, and assessed their antitumoral properties. Specifically, we tested VmCT1 synthetic variants [Arg]3 -VmCT1-NH₂ , [Arg]7 -VmCT1-NH₂ , and [Arg]11 -VmCT1-NH₂ , against Plasmodium gallinaceum sporozoites and MCF-7 mammary cancer cells. Our screen identified peptides [Arg]3 -VmCT1-NH₂ and [Arg]7 -VmCT1-NH₂ as potent antiplasmodial agents (IC₅₀ of 0.57 and 0.51 μmol L-1 , respectively), whereas [Arg]11 -VmCT1-NH₂ did not show activity against P. gallinaceum sporozoites. Interestingly, all peptides presented activity against MCF-7 and displayed lower cytotoxicity toward healthy cells. We demonstrate that increasing the net positive charge of VmCT1, through arginine substitutions, modulates the biological properties of this peptide family yielding novel antiplasmodial and antitumoral molecules.