文献类型：期刊文献

英文题名：Comparison of Inhibitory Activities and Mechanisms of Five Mulberry Plant Bioactive Components against α-Glucosidase

作者：He, Hao[1];Lu, Yan-Hua[1]

机构：[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2013

卷号：61

期号：34

起止页码：8110

外文期刊名：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

收录：;EI(收录号：20133716722285);WOS:【SCI-EXPANDED(收录号:WOS:000323876100014)】；

基金：This work was supported by "the Fundamental Research Funds for the Central Universities", and partially supported by Shanghai Leading Academic Discipline Project (B505), the National Special Fund for State Key Laboratory of Bioreactor Engineering (2060204).

语种：英文

外文关键词：alpha-glucosidase; 1-deoxynojirimycin; resveratrol; oxyresveratrol; cyanidin-3-glucoside; cyanidin-3-rutinoside; interaction

摘要：The a-glucosidase inhibitory effects of five bioactive components, namely I-deoxynojirimycin, cyanidin-3-glucoside, cyanidin-3-rutinoside, resveratrol and oxyresveratrol contained in mulberry (Morus, Moraceae) plants have been compared. Spectroscopy methods were employed to compare their alpha-glucosidase inhibitory mechanisms. The results revealed that 1-deoxynojirimycin (competitive), resveratrol and oxyresveratrol (noncompetitive) were stronger inhibitors than acarbose, while cyanidin-3-glucoside and cyanidin-3-rutinoside (mix competitive and noncompetitive) showed modest activities. IDeoxynojirimycin, resveratrol and oxyresveratrol could quench the fluorescence spectra statically by forming stable complexes, while the quenching of cyanidin-3-rutinoside and cyanidin-3-glucoside belonged to dynamic quenching by the collision of molecules. The interactions between ligands and alpha-glucosidase were mainly driven by hydrophobic force, or hydrogen bonding consequently induced conformational changes and reduced surface hydrophobicity. Docking results suggested that they could bind to alpha-glucosidase at different sites. This work provides useful information for the understanding of the ligands a-glucosidase interactions and identifies oxyresveratrol as a potent alpha-glucosidase inhibitor.