Polyphenols from Flos Trollii inhibit α-amylase and α-glucosidase: Kinetic analysis and mechanistic insights

文献类型： 外文期刊

第一作者： Zhu, Xiaoai

作者： Zhu, Xiaoai;Yan, Kebing;Ye, Xianqing;Ru, Yuan;Niu, Yiying;Liu, Yage;Xi, Jun;Liu, Kunlun;Zhu, Xiaoai;Xiang, Xia

作者机构：

关键词： Polyphenols; alpha-Amylase; alpha-Glucosidase; Inhibition mechanism; Flos Trollii

期刊名称：LWT-FOOD SCIENCE AND TECHNOLOGY （ 影响因子：6.6； 五年影响因子：6.9 ）

ISSN： 0023-6438

年卷期： 2025 年 225 卷

页码：

收录情况： SCI

摘要： The increasing global prevalence of type 2 diabetes mellitus (T2DM) necessitates natural agents that target alpha-amylase and alpha-glucosidase to modulate starch digestion. Although Flos Trollii is a well-documented phytomedicine, its enzymatic inhibition profile remains understudied, particularly with respect to starch-digesting enzymes. This study employed an integrated approach combining UPLC-Q-TOF-MSE, enzyme kinetic, multispectral, and molecular docking simulations to elucidate the inhibitory mechanism of Flos Trollii polyphenols (FTP) on starch-digesting enzymes. UPLC-Q-TOF-MSE identified 10 major polyphenolic compounds. Kinetic analyses indicated that FTP inhibited alpha-amylase in mixed mode (IC50 = 67.70 +/- 9.67 mu g mL-1) and alpha-glucosidase in noncompetitive mode (IC50 = 36.13 +/- 0.23 mu g mL-1). FTP induced dynamic fluorescence quenching, resulting in the formation of enzyme-inhibitor complexes stabilized through hydrogen bonding, van der Waals interactions, and hydrophobic effects. Spectroscopic evidence confirmed that FTP binding triggered shifts in the enzyme structure, ultimately hampering its activity, whereas molecular docking further identified the specific binding sites. This study highlighted the potential of FTP as a nutraceutical for T2DM management.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序