期刊论文

中文

计算机与应用化学

1001-4160

2015

32

10

1177-1181

10.11719/com.app.chem20151006

国家自然科学基金资助项目（31301415）；

本校为第一机构

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 ...