Molecular design, pharmacology and toxicology optimization of antimicrobial peptide from Hydrophis cyanocinctus, Hc-CATH.
- Author:
Jiuxiang GAO
1
;
Yipeng WANG
2
;
Haining YU
1
Author Information
- Publication Type:Journal Article
- Keywords: anti-inflammatory; antibacterial; antibacterial peptide; hydrophobic amino acid; modification
- MeSH: Animals; Anti-Bacterial Agents/pharmacology*; Anti-Infective Agents; Hydrophiidae; Microbial Sensitivity Tests; Pore Forming Cytotoxic Proteins
- From: Chinese Journal of Biotechnology 2021;37(7):2534-2542
- CountryChina
- Language:Chinese
- Abstract: Based on the cathelicidin family antimicrobial peptide Hc-CATH derived from sea snake, the Hc-16 and Hc-15 of 16 and 15 amino acid residues, were designed. By using CCK8, minimal inhibitory concentration, ELISA and bio-layer interferometry assays, their cytotoxicity, antibacterial activity, anti-inflammatory activity, and LPS neutralization activity was examined. Compared with Hc-15, Hc-16 had lower cytotoxicity and better broad-spectrum antibacterial activity against pathogens including clinically resistant bacteria, with the minimum inhibitory concentration of only 4.69 μg/mL. Hc-16 inhibited the expression of inflammatory cytokines of TNF-α and IL-6 induced by LPS, so as to significantly reduce the inflammatory response induced by infection. In addition, structure-activity relationship studies have shown that the phenylalanine at the C- and N-terminals of Hc-16 played a crucial role in its antibacterial and anti-inflammatory activity. Altogether, the designed Hc-16 has an excellent prospect to be developed into a novel antibiotic.
