环糊精与咖啡豆α-半乳糖苷酶的分子对接研究  

Molecular docking of cyclodextrins to coffee-bean α-galactosidase

作　　者：陶佳妮[1] 李赟[1] 姚娣[1] 陈轩[1] 李芳[1,2] 孙威[1] 周坚[1,2] 沈汪洋[1,2] 

机构地区：[1]武汉轻工大学食品科学与工程学院,湖北武汉430023 [2]农产品加工湖北省协同创新中心,湖北武汉430023

出　　处：《计算机与应用化学》2015年第10期1177-1181,共5页Computers and Applied Chemistry

基　　金：国家自然科学基金资助项目(31301415)

摘　　要：通过分子对接方法研究3种主要的环糊精(α-环糊精、β-环糊精及γ-环糊精)与咖啡豆α-半乳糖苷酶的相互作用模型与分子机理。结果表明,咖啡豆α-半乳糖苷酶活性口袋中的关键氨基酸残基为:Trp31、Trp179、Asp200,环糊精中的关键基团为:次甲基上的羟基、亚甲基上的羟基。环糊精覆盖在咖啡豆α-半乳糖苷酶亲水活性空腔的表面,从而抑制其活性,β-环糊精的抑制作用较为明显。分子对接结果为酶法合成α-半乳糖基-环糊精的相互作用研究提供了理论依据。The molecular mechanisms of interactions between coffee-bean a-galactosidase and three cyclodextrins, including alpha-cyclodextrin, beta-cyclodcxtrin and gamma-cyclodcxtrin, were studied in detail by molecular docking. Calculating results showed that Trp 31, Trp 179, and Asp200 in coffee-bean α-galactosidasc wcrc the key amino acid residues in the active pocket. Hydroxyls of the mcthinc and the methane in cyclodextrins were the key groups. Cyclodextrins inhibit coffee-bean a-galactosidase through hydrophilic interactions. Beta-cyclodcxtrin is the most potent inhibitor of α-galactosidase among the three cyclodcxtrins. The molecular docking results provide a theoretical basis for the research about enzymatic inhibitor interaction α-galactopyranosyl-cyclodextrin.

关 键 词：咖啡豆α-半乳糖苷酶 环糊精 结构模型 活性位点 分子对接 

分 类 号：TQ015.9[化学工程] TP391.9[自动化与计算机技术—计算机应用技术]