Molecular mechanism of emodin in inhibiting the activity of Aeromonas hydrophila via AtpE
文献类型： 外文期刊
作者： Zhang, Huimin 1 ; Zhou, Jun 1 ; Li, Xuguang 1 ; Deng, Yanfei 1 ; Ge, Xianping 2 ; Liu, Bo 2 ;
作者机构： 1.Freshwater Fisheries Res Inst Jiangsu Prov, Nanjing, Peoples R China
2.Chinese Acad Fishery Sci, Freshwater Fisheries Res Ctr, Key Lab Freshwater Fisheries & Germplasm Resources, Minist Agr, Wuxi, Peoples R China
关键词： Aeromonas hydrophila; AtpE; emodin; inhibition mechanism; molecular dynamics simulation
期刊名称：NORTH AMERICAN JOURNAL OF AQUACULTURE （ 影响因子：1.0； 五年影响因子：1.4 ）
ISSN： 1522-2055
年卷期： 2024 年 86 卷 2 期
页码：
收录情况： SCI
摘要： Objective: Aeromonas hydrophila, a leading pathogen of aquatic organisms, poses a significant challenge in terms of effective and safe inhibition. Methods: Through the method of experiments and molecular simulations, we dis-covered that emodin effectively inhibits the A. hydrophila via the binding of emodin with AtpE (ATP synthase subunit C). Bacterial inhibition experiments show that emodin effectively inhibits the activity and growth of A. hydrophila. Result: Further molecular docking and molecular dynamics simulation revealed that emodin binds directly to AtpE. More specifically, it binds to certain residues of AtpE, including TYR73, LEU70, ALA13, TYR10, MET17, and ALA14, ultimately leading to inhibition of activity. Conclusion: Consequently, our discovery sheds new light on exploring the molecular mechanism through which emodin displays antimicrobial activity against A. hydrophila.
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