木犀草素抑制酪氨酸酶活性的分子机制  

Molecular Mechanism of Inhibition on Tyrosinase Activity by Luteolin

作　　者：杨城[1] 管骁[1] 韩飞[2] 李景军[3] 廖丽丽 

机构地区：[1]上海理工大学医疗器械与食品学院,上海200093 [2]国家粮食局科学研究院,北京100037 [3]江苏长寿集团股份有限公司,江苏如皋226500 [4]桂林西麦食品集团,广西桂林541004

出　　处：《分析测试学报》2015年第5期532-538,共7页Journal of Instrumental Analysis

基　　金：国家自然科学基金项目(31101348);上海市自然科学基金项目(14ZR1419200)

摘　　要：通过酶抑制动力学实验、荧光猝灭实验以及分子对接技术研究了木犀草素对酪氨酸酶活性的抑制作用。酶抑制动力学实验结果表明:木犀草素是酪氨酸酶的非竞争性抑制剂,抑制常数KI与IC50分别为86mmol/L和778.2μmol/L;荧光猝灭实验结果表明:木犀草素对酪氨酸酶产生静态荧光猝灭作用,疏水作用与氢键作用共同稳定其复合物结构,结合位点数为1;分子对接结果表明:木犀草素在酪氨酸酶疏水口袋边缘与其相互作用,相互作用力包括疏水作用力与氢键。The molecular mechanism of inhibition on tyrosinase activity by luteolin was studied by enzyme kinetics experiment, fluorescence quenching experiment and molecular docking simulation.The enzyme inhibition kinetics experiment results showed that luteolin inhibited the activity of tyrosinase as a non-competitive inhibitor. The inhibition constants KIand IC50 were 86 mmol / L and 778. 2μmol /L,respectively. The fluorescence quenching experiment results showed that the interactions between luteolin and tyrosinase did not change the secondary structure of tyrosinase. As a static quenching,both hydrophobic interaction and hydrogen bonding stabilized the composite structure.Molecular docking simulation showed that the interaction between luteolin and amino acid residues in the hydrophobic pocket of tyrosinase existed. The interaction force mainly included hydrophobic interaction and hydrogen bonding.

关 键 词：木犀草素 酪氨酸酶 抑制作用 荧光猝灭 分子对接 

分 类 号：O657[理学—分析化学] TL271[理学—化学]