文献类型：期刊文献

英文题名：α-Glucosidase inhibition activity and mechanism of phenolic compounds extracted from Gleditsia sinensis Lam.

作者：Liu, Yong[1] Deng, Yejun[1] Wang, Xiang[1] Zhang, Caihong[1,2] Huang, Lixin[1,2,3,4,5] Xie, Pujun[1,2,3,4,5]

通信作者：Huang, LX[1];Xie, PJ[1];Huang, LX[2];Xie, PJ[2];Huang, LX[3];Xie, PJ[3];Huang, LX[4];Xie, PJ[4];Huang, LX[5];Xie, PJ[5]

机构：[1]Chinese Acad Forestry, Inst Chem Ind Forest Prod, Natl Key Lab Dev & Utilizat Forest Food Resources, Nanjing 210042, Peoples R China;[2]Nanjing Forestry Univ, Int Innovat Ctr Forest Chem & Mat, Jiangsu Co Innovat Ctr Efficient Proc & Utilizat F, Nanjing 210042, Peoples R China;[3]Key Lab Biomass Energy & Mat, Nanjing 210042, Jiangsu, Peoples R China;[4]Natl Forestry & Grassland Adm, Key Lab Chem Engn Forest Prod, Nanjing 210042, Peoples R China;[5]Natl Engn Res Ctr Low Carbon Proc & Utilizat Fores, Nanjing 210042, Peoples R China

年份：2026

外文期刊名：JOURNAL OF FOOD MEASUREMENT AND CHARACTERIZATION

收录：;EI(收录号：20260419960807);Scopus(收录号：2-s2.0-105028192741);WOS:【SCI-EXPANDED(收录号:WOS:001665567400001)】；

基金：This work was supported by the Fundamental Research Funds of the Chinese Academy of Forestry (CAFYBB2022XB002-2), and the National Natural Science Foundation of China (grant number: 32171732).

语种：英文

外文关键词：alpha-Glucosidase inhibition; Gleditsia sinensis Lam.; Screening process; Correlation analysis; Fisetin; Inhibitory mechanism

摘要：Inhibiting alpha-glucosidase activity by secondary metabolites has been confirmed as an effective strategy for treating type 2 diabetes mellitus (T2DM). alpha-Glucosidase inhibitory activity was determined by different parts of Gleditsia sinensis Lam. (GSL) extracts. The thorn of the GSL methanol extract exhibited the highest activity (IC50 = 0.21 mg/mL). Eleven potential alpha-glucosidase inhibitors were detected by Ultra Performance Liquid Chromatography Quadrupole Time of Flight Mass Spectrometry, and fisetin was screened as the dominant compound (IC50 = 0.211 mu M) through virtual screening, correlation analysis, and inhibitory assay. Fluorescence quenching experiment explained that fisetin inhibited alpha-glucosidase through hydrogen bonds and hydrophobic forces in a reversible and non-competitive mode. Three-dimensional fluorescence and circular dichroism demonstrated that fisetin modified the amino acids' microenvironment and disrupted the hydrogen-bonded network of alpha-glucosidase. alpha-Glucosidase was bounded with fisetin by hydrogen (Thr448, His515, Asp346, and Gln531) and hydrophobic residues (His515, Lys352, and Ala349) simulated by molecular docking. This study points out the fisetin's inhibitory mechanism of alpha-glucosidase, indicating that it is a promising natural ingredient in T2DM treatment.