Peptide name : VmCT1

Source/Organism : Scorpions, Morelos, located in South-Central Mexico

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 13

C-terminal modification: Not found

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Anti-bacterial activity; Hemolytic activity

Amino acid composition bar chart :

Molecular mass : 1451.7093 Dalton

Aliphatic index : 1.2

Instability index : 30.4077

Hydrophobicity (GRAVY) : 1.2077

Isoelectric point : 8.7501

Charge (pH 7) : 0.7591

Aromaticity : 0.230

Molar extinction coefficient (cysteine, cystine): (5500, 5500)

Hydrophobic/hydrophilic ratio : 3.33333333

hydrophobic moment : 1.4872

Missing amino acid : C,R,H,Q,T,P,M,I,E,D,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): (0.3, 0.2, 0.5)

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](CC(N)=O)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 : Ramírez-Carreto S, et al. Gene cloning and functional characterization of four novel antimicrobial-like peptides from scorpions of the family Vaejovidae. Peptides. 2012; 34:290-5. doi: 10.1016/j.peptides.2012.02.002

Paper title : Gene cloning and functional characterization of four novel antimicrobial-like peptides from scorpions of the family Vaejovidae.

Doi : https://doi.org/10.1016/j.peptides.2012.02.002

Abstract : From the cDNA libraries made from the venom glands of two scorpions belonging to the Vaejovidae family, four different putative non disulfide-bridged antimicrobial peptides were identified: VmCT1 and VmCT2 from Vaejovis mexicanus smithi plus VsCT1 and VsCT2 from Vaejovis subcristatus. These short peptides (with only 13 amino acid residues each) share important amino acid sequence similarities among themselves and with other reported antimicrobial peptides, but their biological activities vary dramatically. This communication reports the cloning, chemical synthesis and characterization of these peptides. Two peptides, VmCT1 and VmCT2 showed broad-spectrum antibacterial activity with minimum inhibitory concentrations MICs in the range of 5-25 μM and 10-20 μM respectively, whereas their hemolytic activity at these concentrations was low. Structure-function relationships that might determine the differences in activities are discussed.