黄嘌呤氧化酶
化学
分子动力学
对接(动物)
动能
光谱学
计算化学
生物物理学
立体化学
生物化学
酶
生物
物理
医学
护理部
量子力学
作者
Xiaoze Liu,Qian Zhang,Jingwen Chen,R. D. Fu,Xue Lin,Shaobo Zhou,Lu Wang
标识
DOI:10.1016/j.ijbiomac.2024.136231
摘要
Catechins compounds from tea have demonstrated significant inhibitory effects on xanthine oxidase (XOD). However, the precise inhibitory mechanisms of the main catechins on XOD remain to be fully elucidated. This study explored the inhibition mechanisms and binding characteristics of five catechins (GC, EGC, EC, EGCG, and ECG) on XOD through a combination of inhibition kinetics, multi-spectroscopy analysis, molecular docking, and dynamics simulations. Among the catechins, EGCG and ECG exhibited the most potent inhibitory activities against XOD. All five catechins were found to exhibit mixed inhibition, affecting the hydrophobic groups and secondary structure of XOD predominantly through hydrophobic interactions and hydrogen bonding. Molecular dynamics simulations revealed that a 3,4,5-trihydroxybenzoic acid moiety at C
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