基于分子对接技术探究黄酮类化合物对α-葡萄糖苷酶抑制作用的机制  

Mechanism of flavonoids inhibitingα-glucosidase explored based on molecular docking technology

作　　者：席晓萌 姜云鸽 王琳[2] 黄相中[1,2] 田凯[1,2] XI Xiao-meng;JIANG Yun-ge;WANG lin;HUANG Xiang-zhong;TIAN kai(Laboratory of Theoretical and Computational Chemistry,Yunnan Minzu University,Kunming 650500,China;Key Laboratory of Chemistry in Ethnic Medicinal Resources,State Ethnic Affairs Commission and Ministryof Education of China,Yunnan Minzu University,Kunming 650500,China)

机构地区：[1]云南民族大学理论与计算化学实验室,云南昆明650500 [2]云南民族大学民族药资源化学国家民族事务委员会-教育部重点实验室,云南昆明650500

出　　处：《云南民族大学学报（自然科学版）》2021年第6期525-531,共7页Journal of Yunnan Minzu University:Natural Sciences Edition

基　　金：国家自然科学基金(81960783);云南省高校传统彝药药效物质基础研究科技创新团队项目.

摘　　要：采用分子对接的方法将实验室获得的44个黄酮类化合物与α-葡萄糖苷酶蛋白进行对接分析,应用Discovery Studio 2.5软件中的Dock Ligand(Libdcok)对接方法,得到LibDock Score以及相应的活性位点,以LibDock Score大于130为筛选标准,得到了排名前10的对接结果,进一步筛选出4种可以有效抑制α-葡萄糖苷酶活性的黄酮类药物.将对接结果以二维图和三维图形式进行展示,推测出ARG1591、ARG1410和GLU1397可能为α-葡萄糖苷酶的活性位点残基,证实了上述介绍的分子优化对接方法来进行相关实验是具有可行性的,能够为新型α-葡萄糖苷酶抑制剂药物的研究提供一定的理论依据.A total of 44 flavonoids obtained in the laboratory were butted againstα-glucosidase protein by molecular docking,and LibDock Score and its corresponding active sites were obtained byDock Ligand(Libdcok)method in Discovery Studio 2.5 software.With LibDock Score greater than 130 as the screening criterion,the top ten docking results were obtained,and four flavonoid drugs that could effectively inhibitα-glucosidase activity were further screened out.The docking results were shown in two-dimensional and three-dimensional figures,and it was speculated that ARG1591,ARG1410 and GLU1397 might be the active site residues ofα-glucosidase,which confirmed the feasibility of the molecular optimization docking method described above for related experiments and provided a certain theoretical basis for the research of newα-glucosidase inhibitor drugs.

关 键 词：分子对接 Discovery Studio 2.5 黄酮类化合物 Α-葡萄糖苷酶抑制剂 

分 类 号：R914.2[医药卫生—药物化学]