Inhibition Mechanism of Barbaloin on Mushroom TyurOSinase:A Molecular Docking Model Supported by Fluorescence Quenching
Tyrosinase inhibitors have wide applications in cosmetics,food and agriculture.Inhibition mechanism of barbaloin on mushroom tyrosinase has been investigated by molecular docking and fluorescence quenching.The results showed that barbaloin is an efficient inhibitor on mushroom tyrosinase.A molecular docking model of barbaloin binding to mushroom tyrosinase was simulated.One barbaloin molecule inserts into the active site cavity of tyrosinase,and the position of barbaloin molecule is nearer to tryptophan than to tyrosine.The complex ofbarbaloin and tyrosinase is stabled by 7 hydrogen bonds and hydrophobic force with the residues on the wall of catalytic cavity.As supported by the fluorescence quenching results,the molecular docking model can be considered as a mechanism model.Barbaloin quenched the mushroom tryosinase fluorescence through a static mechanism by binding to tyrosinase with the negative enthalpy change and the positive entropy change,and had a stronger fluorescence quenching effect on tryptophan than tyrosine.
Barbaloin Tyrosinase inhibition Fluorescence quenching Molecular docking
MU Yan SHEN Xing LI Lin HU Song-Qing
Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety,School of Light Industry and Food Sciences,South China University of technology,Guangzhou,Guangdong,510640,China
国内会议
广州
英文
531-539
2015-07-03（万方平台首次上网日期，不代表论文的发表时间）