Exploring the mechanism and inhibitory effect of robinin on xanthine oxidase using multi-spectroscopy and molecular dynamics simulation methods

文献类型： 外文期刊

第一作者： Liu, Mengyao

作者： Liu, Mengyao;Wu, Xinning;Chen, Hualei;Pan, Fei;Wang, Wenqian;Fang, Xiaoming;Peng, Wenjun;Li, Xiangxin;Tian, Wenli

作者机构：

关键词： Robinin; Xanthine oxidase; Multispectroscopy; Inhibitory mechanism; Molecular docking

期刊名称：JOURNAL OF MOLECULAR LIQUIDS （ 影响因子：5.3； 五年影响因子：5.1 ）

ISSN： 0167-7322

年卷期： 2024 年 408 卷

页码：

收录情况： SCI

摘要： Xanthine oxidase (XOD) is a key enzyme in purine metabolism that is tightly associated with hyperuricemia (HUA). Natural flavonoids can inhibit XOD activity. In this study, the inhibitory activity and mechanism of the novel flavonoid robinin on XOD were analyzed using enzyme inhibition kinetics, multispectral techniques, molecular docking, and molecular dynamics (MD) simulations. Robinin reversibly inhibited the activity of XOD in a mixed competitive manner, with an IC50 value of 31.79 +/- 0.15 mu g/mL. Moreover, robinin spontaneously binds to a specific site on XOD and effectively quenches its intrinsic fluorescence via a single static quenching mechanism. The combination of XOD and robinin induced secondary structure rearrangement and conformational changes in XOD and prevented the entry of substrates, thus producing a strong inhibitory effect. Molecular docking and MD simulation revealed that robinin mainly binds to XOD through hydrogen bonding and hydrophobic interactions to form more stable complexes with a binding energy of -7.4 kcal/mol. Overall, this study established a theoretical reference for robinin as a promising natural XOD inhibitor for relieving HUA.

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