水杨酸
金黄色葡萄球菌
免疫印迹
非竞争性抑制剂
生物化学
体内
化学
微生物学
药理学
生物
细菌
非竞争性抑制
酶
生物技术
遗传学
基因
作者
Yijing Jiang,Juan Hou,Chang Liu,Chunhui Zhao,Yangming Xu,Song Wu,Zunhua Shu,Bingmei Wang
出处
期刊:ChemMedChem
[Wiley]
日期:2023-09-27
卷期号:18 (22)
被引量:1
标识
DOI:10.1002/cmdc.202300302
摘要
Abstract The massive use of antibiotics has resulted in an alarming increase in antibiotic resistance in Staphylococcus aureus ( S. aureus ). This study aimed to identify the inhibitory effect of salicin on S. aureus . Coagulase (Coa) activity was assessed using in vitro Coa assays and Western blot, thermal shift assay (TSA), fluorescence quenching and molecular docking experiments were conducted to verify the interaction between salicin and Coa. An in vivo mouse pneumonia model demonstrated that salicin can reduce the virulence of S. aureus. In vitro Coa assays elucidated that salicin directly inhibited Coa activity. The Western blot and TSA results suggested that salicin did not block the expression of Coa but affected the thermal stability of the protein by binding to Coa. The fluorescence quenching, molecular docking and molecular dynamics assays have found that the most promising binding site between salicin and Coa was GLN‐97. The pneumonia model of mice infected with S. aureus revealed that salicin could not only reduce the content of lung bacteria in mice but also prolong their survival. Salicin was identified as a novel anti‐infective candidate compound with the potential to target Coa and inhibit its activity by binding to it, which would facilitate the development of roadmaps for future research.
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