首页 | 本学科首页   官方微博 | 高级检索  
     检索      


Kinetics and Computational Docking Studies on the Inhibition of Tyrosinase Induced by Oxymatrine
Authors:Xiao-Xia Liu  Shi-Qing Sun  Yu-Jie Wang  Wei Xu  Yi-Fang Wang  Daeui Park  Hai-Meng Zhou  Hong-Yan Han
Institution:1. College of Biological, Chemical Sciences and Engineering, Jiaxing University, Jiaxing, 314001, People’s Republic of China
2. Molecular Inflammation Research Center for Aging Intervention (MRCA), College of Pharmacy, Pusan National University, Busan, 609-735, Korea
3. Zhejiang Provincial Key Laboratory of Applied Enzymology, Yangtze Delta Region Institute of Tsinghua University, Jiaxing, 314006, People’s Republic of China
4. School of Biology and Basic Medical Sciences, Soochow University, Suzhou, 215123, People’s Republic of China
Abstract:A combination of enzymatic inhibition kinetics and computational prediction was employed to search for an effective inhibitor of tyrosinase. We found that oxymatrine significantly inhibited tyrosinase, and that this reaction was not accompanied by detectable conformational changes. Kinetic analysis showed that oxymatrine reversibly inhibited tyrosinase in a mixed-type manner. Measurements of intrinsic and ANS-binding fluorescences showed that oxymatrine did not induce any conspicuous changes in the tertiary structure. We also conducted a docking simulation between tyrosinase and oxymatrine using two docking programs, Dock6.3 and AutoDock4.2 (binding energy was ?118.81 kcal/mol for Dock6 and ?8.04 kcal/mol for AutoDock4). The results also suggested that oxymatrine interacts mostly with the residues of CYS83 and HIS263 in the active site of tyrosinase. This strategy of predicting tyrosinase inhibition by simulation of docking coupling with kinetics may prove useful in screening for potential tyrosinase inhibitors. Knowledge of tyrosinase inhibition can provide medical, cosmetic, and agricultural applications. Our study suggests that oxymatrine is an important agent for various applications related to pigment formation.
Keywords:
本文献已被 SpringerLink 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号