Peptide name : Brevinin-1Ha

Source/Organism : Analogue of Brevinin-1H

Linear/Cyclic : Linear

Chirality : L

Peptide length: 21

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information:

Assay type : MTT assay

Assay time : 24-h

Activity : IC50 = 186.9 µM

Cell line : PC-3

Cancer type : Prostate Cancer

Other activity : Antimicrobial

Amino acid composition bar chart :

Molecular mass : 2321.9314 Dalton

Aliphatic index : 1.3

Instability index : 11.6952

Hydrophobicity (GRAVY) : 1.081

Isoelectric point : 9.8507

Charge (pH 7) : 3.7373

Aromaticity : 9.523

Molar extinction coefficient (cysteine, cystine): (2, 1)

Hydrophobic/hydrophilic ratio : 2.5

hydrophobic moment : -0.811

Missing amino acid : D,E,H,M,N,Q,S,W,Y

Most occurring amino acid : L

Most occurring amino acid frequency : 4

Least occurring amino acid : G

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (42., 9.5, 52.)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@@H](N)Cc1ccccc1)C(C)C)[C@@H](C)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)O)C(C)C)[C@@H](C)O

1 : Pei X, et al. Characterisation of a novel peptide, Brevinin-1H, from the skin secretion of Amolops hainanensis and rational design of several analogues. Chem Biol Drug Des. 2021; 97:273-282. doi: 10.1111/cbdd.13779

Paper title : Characterisation of a novel peptide, Brevinin-1H, from the skin secretion of Amolops hainanensis and rational design of several analogues.

Doi : https://doi.org/10.1111/cbdd.13779

Abstract : As drug-resistant bacteria have become a serious health problem and have caused thousands of deaths, finding new antibiotics has become an urgent research priority. A novel antimicrobial peptide, named Brevinin-1H, was identified in the skin secretion of Amolops hainanensis through 'shotgun' cloning. It has broad-spectrum antimicrobial activity against tested micro-organisms and has anticancer cell activity. To improve its bioactivity and decrease its cytotoxicity, two structural analogues-Brevinin-1Ha and Brevinin-1HY-were designed based on the secondary structure of the natural peptide. Brevinin-1HY, in which tyrosine substituted Pro11 , had similar activity to the natural peptide against Gram-negative bacteria and cancer cells, but showed a dramatic increase in haemolytic activity and cytotoxicity at its minimum inhibitory concentration. Brevinin-1Ha, which transferred the Rana-box from the C-terminal to a central position, had significantly decreased haemolytic activity, but also in antimicrobial and anticancer activity. The present data suggest that increasing the proportion of α-helix structure in an AMP can increase its target micro-organism bioactivity to some extent.