Inhibition of α-amylase activity by quercetin via multi-spectroscopic and molecular docking approaches

文献类型： 外文期刊

第一作者： Huang, Meigui

作者： Huang, Meigui;Xiao, Qiao;Li, Yonghong;Ahmad, Mehraj;Tang, Jiajia;Liao, Qiuhong;Tan, Chen

作者机构：

关键词： Quercetin; Inhibition mechanism; alpha-Amylase; Molecular docking

期刊名称：FOOD BIOSCIENCE （ 影响因子：5.9； 五年影响因子：6.1 ）

ISSN： 2212-4292

年卷期： 2024 年 61 卷

页码：

收录情况： SCI

摘要： The quercetin-induced inhibition of alpha-amylase activity was comprehensively studied using various spectroscopic methods, including UV-Visible, fluorescence, and Fourier-transform infrared spectroscopy. Quercetin acted as a mixed-type inhibitor, and its binding altered the kinetic properties of alpha-amylase. Quercetin exhibited static binding with alpha-amylase, as evidenced by a higher Stern-Volmer constant (KSV) K SV ) at 298 K (9.56 +/- 0.63 x 103 3 L/ mol) compared to the K SV value at 318 K (5.56 +/- 0.48 x 103 3 L/mol). Additionally, quercetin induced conformational changes in the hydrophobic micro-environment surrounding the tryptophan and tyrosine residues of alpha-amylase, as indicated by fluorescence spectroscopy. Hydrophobic interactions primarily drove the spontaneous binding between alpha-amylase and quercetin from thermodynamic data. Molecular docking studies supported the role of hydrogen bonds (Asp197 and Gln63) and hydrophobic interactions (with active site residues Ala198, Leu165, and Trp59) in the complex formation. These findings provide a detailed understanding of how quercetin inhibits alpha-amylase activity, reinforcing its potential as a glycemic controller in food formulations.

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