数字农科院2.0

Engineered Peptides Harboring Cation Motifs Against Multidrug-Resistant Bacteria

文献类型： 外文期刊

作者： Shang, Lu;Chen, Chan;Sun, Rui;Guo, Juan;Liu, Jing;Wang, Mi;Zhang, Lifang;Fei, Chenzhong;Xue, Feiqun;Liu, Yingchun;Gu, Feng

作者机构：

关键词： antibiotic resistance;multidrug-resistant pathogens;antimicrobial peptide;biosafety;biofilm

期刊名称： ACS APPLIED MATERIALS & INTERFACES

ISSN： 1944-8244

年卷期： 2024 年 16 卷 5 期

页码：

收录情况： SCIE（2024版） ; ; EI（2024版）

摘要： Multidrug-resistant (MDR) pathogens pose a serious threat to the health and life of humans, necessitating the development of new antimicrobial agents. Herein, we develop and characterize a panel of nine amino acid peptides with a cation end motif. Bioactivity analysis revealed that the short peptide containing RWWWR as a central motif harboring mirror structure KXR unit displayed not only high activity against MDR planktonic bacteria but also a clearance rate of 92.33% +/- 0.58% against mature biofilm. Mechanically, the target peptide (KLR) killed pathogens by excessively accumulating reactive oxygen species and physically disrupting membranes, thereby enhancing its robustness for controlling drug resistance. In the animal model of sepsis infection by MDR bacteria, the peptide KLR exhibited strong therapeutic effects. Collectively, this study provided the dominant structure of short antimicrobial peptides (AMPs) to replenish our arsenals for combating bacterial infections and illustrated what could be harnessed as a new agent for fighting MDR bacteria.

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