Studies on the interaction mechanism between xanthine oxidase and osmundacetone: Molecular docking, multi-spectroscopy and dynamical simulation

文献类型： 外文期刊

第一作者： Song, Jiling

作者： Song, Jiling;Chen, Jiahui;Wang, Zhanwei;Zhang, Yong;Wang, Jing;Chen, Minghui;Cui, Jing;Wang, Jing;Shi, Dongfang;Meng, Fanlei;Zhang, Yong;Cui, Jing;Wang, Jing;Shi, Dongfang;Wang, Jing;Shi, Dongfang

作者机构：

关键词： Inonotus obliquus; Osmundacetone; Inhibition kinetics; Fluorescence quenching; Molecular docking; Xanthine oxidase inhibitor

期刊名称：SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY （ 影响因子：4.4； 五年影响因子：3.9 ）

ISSN： 1386-1425

年卷期： 2023 年 299 卷

页码：

收录情况： SCI

摘要： Xanthine oxidase (XO) is a key enzyme in uric acid production, and its molybdopterin (Mo-Pt) domain is an important catalytic center when xanthine and hypoxanthine are oxidated. It is found that the extract of Inonotus obliquus has an inhibitory effect on XO. In this study, five key chemical compounds were initially identified using liquid chromatography-mass spectrometry (LC-MS), and two compounds, osmundacetone ((3E)-4-(3,4-dihydroxyphenyl)-3-buten-2-one) and protocatechuic aldehyde (3,4-dihydroxybenzaldehyde), were screened as the XO inhibitors by ultrafiltration technology. Osmundacetone bound XO strongly and competitively inhibited XO with a half-maximal inhibitory concentration of 129.08 +/- 1.71 mu M, and its inhibition mechanism, was investigated. Osmundacetone and XO via static quenching and spontaneously bound with XO with high affinity, primarily via hydrophobic interactions and hydrogen bonds. Molecular docking studies showed that osmunda-cetone was inserted into the Mo-Pt center and interacted with hydrophobic residues of Phe911, Gly913, Phe914, Ser1008, Phe1009, Thr1010, Val1011, and Ala1079 of XO. In summary, these findings suggest that provide theoretical basis for the research and development of XO inhibitors from Inonotus obliquus.

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