Self-assembling anti-Gram-negative bacterial peptide derivatives with potent broad-spectrum antimicrobial activity

文献类型： 外文期刊

第一作者： Yang, Hongyan

作者： Yang, Hongyan;Yuan, Libo;Du, Heng;Lu, Kui;Wang, Lan;Lu, Kui;Pan, Fei;Zhang, Pei

作者机构：

关键词： Antimicrobial peptides; Amphiphilic lipopeptide; Self-assembly; Activity; Mechanism

期刊名称：LWT-FOOD SCIENCE AND TECHNOLOGY （ 影响因子：6.0； 五年影响因子：6.0 ）

ISSN： 0023-6438

年卷期： 2023 年 185 卷

页码：

收录情况： SCI

摘要： Food contamination caused by bacteria is an important challenge in the food industry. In this study, the peptide derivative C12-CL5 was produced by attaching a 12-carbon saturated fatty acid to the N-terminus of the anti Gram-negative bacterial peptide CL5. The amphiphilic lipopeptide C12-CL5 self-assembled into core-shell nanostructures at concentrations above its critical aggregation concentration. It was found that the self assembling C12-CL5 showed potent activity against both Gram-negative and Gram-positive bacteria, with minimum inhibitory concentrations of 4-32 & mu;M. Moreover, C12-CL5 exhibited good thermal stability, excellent salt tolerance, as well as strong and rapid killing kinetics. Studies on the antimicrobial mechanism of C12-CL5 indicated that it could disrupt cell membranes, leading to leakage of cellular contents and ultimately to bacterial death. This study revealed that the self-assembly of antimicrobial peptides improved their antimicrobial activity and spectrum. It provides the insights and basis for the development of potent and broad-spectrum antimicrobial peptides for use, e.g., in the food industry.

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