Polyphenols from Flos Trollii inhibit α-amylase and α-glucosidase: Kinetic analysis and mechanistic insights
文献类型： 外文期刊
作者： Zhu, Xiaoai 1 ; Yan, Kebing 1 ; Ye, Xianqing 1 ; Xiang, Xia 2 ; Ru, Yuan 1 ; Niu, Yiying 1 ; Liu, Yage 1 ; Xi, Jun 1 ; Liu, Kunlun 1 ;
作者机构： 1.Henan Univ Technol, Coll Food Sci & Engn, Zhengzhou 450001, Peoples R China
2.Chinese Acad Agr Sci, Minist Agr & Rural Affairs, Key Lab Biol & Genet Improvement Oil Crops, Key Lab Oilseeds Proc,Oil Crops Res Inst, Wuhan 430062, Peoples R China
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.
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