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文章构建了α-葡萄糖苷酶的三维结构,并研究其与抑制剂分子的作用方式。以蜡状芽孢杆菌聚-1,6-葡萄糖苷酶的晶体结构为模板,利用同源模建法对α-葡萄糖苷酶的三维结构进行了模拟,并采用分子动力学方法对模型进行了修正和优化。在此基础上,使用InsightII软件包中的Biopolymer,Discover,Docking等模块,研究α-葡萄糖苷酶和其抑制剂伏格列波糖、米格列醇相互作用的结合位点和作用性质。模建出的α-葡萄糖苷酶三维结构,其可靠性经Ramachandran图和verify-3D图验证。α-葡萄糖苷酶与抑制剂主要通过氢键作用和疏水所用结合在一起。α-葡萄糖苷酶模型的建立和分子间作用的研究为α-葡萄糖苷酶抑制剂的虚拟筛选和对现有的抑制剂进行结构改造提供了一些有用的信息。
The article builds the three-dimensional structure of α-glucosidase and studies its mode of action with inhibitor molecules. The crystal structure of Bacillus cereus poly-1,6-glucosidase was used as a template to simulate the three-dimensional structure of α-glucosidase by homology modeling and the molecular dynamics method was used to correct the model And optimized. Based on this, the binding sites and the action properties of α-glucosidase and its inhibitor voglibose and miglitol were studied by using the modules such as Biopolymer, Discover and Docking in InsightII software package. The three-dimensional structure of α-glucosidase was constructed and its reliability was verified by Ramachandran map and verify-3D map. Alpha-glucosidase and inhibitors are mainly combined by hydrogen bonding and hydrophobicity. The establishment of α-glucosidase model and the study of intermolecular interaction provide some useful information for the virtual screening of α-glucosidase inhibitors and the structural modification of existing inhibitors.