Membrane interaction and antibacterial properties of chensinin-1, an antimicrobial peptide with atypical structural features from the skin of Rana chensinensis

Applied Microbiology and Biotechnology
De-Jing ShangLi Sun

Abstract

Many antimicrobial peptides from amphibian skin have been purified and structurally characterized and may be developed as therapeutic agents. Here we describe the antibacterial properties and membrane interaction of chensinin-1, a cationic arginine/histidine-rich antimicrobial peptide, from the skin secretions of Rana chensinensis. The amino acid composition, sequence, and atypical structure of chensinin-1 differ from other known antimicrobial peptides from amphibian skin. Chensinin-1 exhibited selective antimicrobial activity against Gram-positive bacteria, was inactive against Gram-negative bacteria, and had no hemolytic activity on human erythrocytes. The CD spectra for chensinin-1 indicated that the peptide adopted an aperiodic structure in water and a conformational structure with 20 % β-strands, 8 % α-helices, and the remaining majority of random coils in the trifluoroethanol or SDS solutions. Time-kill kinetics against Gram-positive Bacillus cereus demonstrated that chensinin-1 was rapidly bactericidal at 2× MIC and PAE was found to be >5 h. Chensinin-1 caused rapid and large dye leakage from negatively charged model vesicles. Furthermore, membrane permeation assays on intact B. cereus indicated that chensinin-1 induced ...Continue Reading

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Citations

Apr 10, 2016·Acta Biomaterialia·Weibing DongDejing Shang
May 12, 2016·Interdisciplinary Sciences, Computational Life Sciences·Rui-Fang LiChao-Nan Li
Aug 8, 2019·Molecular Oral Microbiology·Maryta N SztukowskaDonald R Demuth

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