Computational Study on the Comparative Differences in the Activity of Inhibitors of Human versus Rat Alpha-Glucosidase  

作　　者：Shinya Nakamura Kazuko Shimada Genzoh Tanabe Osamu Muraoka Isao Nakanishi 

机构地区：[1]Department of Pharmaceutical Sciences, Kindai University, Higashiosaka, Japan

出　　处：《Open Journal of Medicinal Chemistry》2017年第2期19-28,共10页药物化学期刊（英文）

摘　　要：Differences between the inhibitory activities of specific compounds on analogous enzymes isolated from different animal species are one of the critical issues to evaluate when exploring structure-activity relationships. The activity of acarbose is about ten times stronger in rat than in human, and that of neosalacinol is similar in both species. Binding affinities of acarbose and neosalacinol to four catalytic domains of alpha-glucosidases in human and rat were compared to investigate the cause of activity differences among species. Species difference was brought about complicatedly by the balance of interaction with four domains, and the result was indicated that larger ligand would show larger species difference in activity.Differences between the inhibitory activities of specific compounds on analogous enzymes isolated from different animal species are one of the critical issues to evaluate when exploring structure-activity relationships. The activity of acarbose is about ten times stronger in rat than in human, and that of neosalacinol is similar in both species. Binding affinities of acarbose and neosalacinol to four catalytic domains of alpha-glucosidases in human and rat were compared to investigate the cause of activity differences among species. Species difference was brought about complicatedly by the balance of interaction with four domains, and the result was indicated that larger ligand would show larger species difference in activity.

关 键 词：HOMOLOGY Modeling MM/PBSA ALPHA-GLUCOSIDASE Salacinol ACARBOSE Species DIFFERENCE 

分 类 号：R73[医药卫生—肿瘤]