文献类型： 外文期刊

作者： Liu, Jiang ¹ ; Wang, Xiansheng ³ ; Geng, Sheng ¹ ; Liu, Benguo ¹ ; Liang, Guizhao ² ;

作者机构： 1.Henan Inst Sci & Technol, Sch Food Sci, Xinxiang 453003, Peoples R China

2.Chongqing Univ, Key Lab Biorheol Sci & Technol, Minist Educ, Bioengn Coll, Chongqing 400044, Peoples R China

3.Jiangsu Acad Agr Sci, Inst Food Crops, Minist Agr, Nanjing Stn,DUS Testing Ctr New Plant Varieties, Nanjing 210014, Jiangsu, Peoples R China

关键词： Taxifolin;alpha-Glucosidase;Inhibition mechanism;Spectrofluorimetry;Molecular docking

期刊名称：NATURAL PRODUCT COMMUNICATIONS （ 影响因子：0.986； 五年影响因子：1.068 ）

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收录情况： SCI

摘要： The alpha-glucosidase inhibitory activity and behavior of taxifolin was first investigated by spectrofluorimetry and molecular docking. It was found that taxifolin inhibits alpha-glucosidase in a competitive manner with the IC50 value of 0.16 mg/mL. The intrinsic fluorescence quenching of alpha-glucosidase in the presence of taxifolin was observed by the static quenching mechanism. According to the thermodynamic study, the complex of taxifolin and alpha-glucosidase was maintained by van der Waals and hydrogen bonding. The binding mode provided by molecular docking simulation indicated the existence of hydrogen bonding between taxifolin and the amino acid residues of a-glucosidase (Glu429, Asp 568 and Glu771), which coincided with the result of fluorescence analysis.