Highly selective performance of rationally designed antimicrobial peptides based on ponericin-W1

抗菌肽 抗菌剂 抗菌活性 化学 细菌 氨基酸 生物化学 抗生素 肽序列 阳离子聚合 抗菌肽 体内 体外 抗菌剂 组合化学 生物 有机化学 生物技术 基因 遗传学
作者
Songwei Lv,Jing‐Fang Wang,Rongrong You,Suyu Liu,Yujie Ding,Roja Hadianamrei,Mhd Anas Tomeh,Fang Pan,Zhiqiang Cai,Xiubo Zhao
出处
期刊:Biomaterials Science [The Royal Society of Chemistry]
卷期号:10 (17): 4848-4865 被引量:11
标识
DOI:10.1039/d2bm00744d
摘要

Antimicrobial peptides (AMPs) or host-defence peptides act by penetrating and disrupting the bacterial membranes and are therefore less prone to antimicrobial resistance (AMR) compared to conventional antibiotics. However, there are still many challenges in the clinical application of the naturally occurring AMPs which necessitates further studies to establish the relationship between the chemical structure of AMPs and their antimicrobial activity and selectivity. Herein, we report a study on the relationship between the chemical structure and the biological activity of a series of rationally designed AMPs derived from Ponericin-W1, a naturally occurring AMP from ants. The peptides were designed by modification of the hydrophobic and hydrophilic regions of the lead peptide sequence in a systematic way. Their antibacterial and hemolytic activities were determined in vitro. The antibacterial activity of a representative peptide, At5 was also tested in a mouse model of skin wound infection. Furthermore, the relationship between the physicochemical properties of the peptides and their antibacterial activity was investigated. Replacing the cationic amino acids in the hydrophobic region of the peptides with hydrophobic amino acids enhanced their antibacterial activity and increasing the number of cationic amino acids in the hydrophilic region reduced their toxicity to human red blood cells and thus improved their selectivity for bacteria. Four of the designed peptides, coded as At3, At5, At8, and At10, displayed considerable antibacterial activity and high selectivity for bacteria. At5 also accelerated the wound healing in mice indicating high in vivo efficiency of this peptide. The peptides were more effective against Gram-negative bacteria and no AMR was developed against them in the bacteria even after 25 generations. The results from this study can provide a better understanding of the structural features required for strong antibacterial activity and selectivity, and serve as a guide for the future rational design of AMPs.
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