天然产物研究与开发2018，Vol.30Issue(1)：33-40,83,9.DOI:10.16333/j.1001-6880.2018.1.006
光谱法和分子对接研究二氢杨梅素与人血清白蛋白相互作用
The Interaction of Dihydromyricetin with Human Serum Albumin by Spectroscopic Methodologies and Molecular Docking
摘要
Abstract
The interaction of dihydromyricetin (DMY) with human serum albumin (HSA) was investigated by spectroscopic methodologies and molecular docking.The fluorescence spectral results showed that HSA fluorescence was quenched regularly with the addition of DMY,the quenching mechanism may be a static fluorescence quenching procedue.All the magnitude of binding constants (KA) were larger than 105 L/mol and the number of binding sites (n) in the binary system were approximate to 1 in different temperature.According to thermodynamic parameters of Van't Hoff equation,it could be suggested the binding process of DMY with HSA was spontaneous and the main interaction force of DMY with HSA was electrostatic force.The binding distance (r) between the DMY and HSA was calculated to be about 3.32 nm based on the theory of Fisrster's nonradiation energy transfer,which indicated that the energy trasfer from HSA to DMY occurs with high possibility.The synchronous and 3D florescence spectroscopy demonstrated that the secondary conformation of HSA has been changed after interaction with DMY.From the result of site marker competitive experiments and the molecular docking,it could be deduced that DMY was inserted into the subdomain ⅡA (site Ⅰ) of HSA.关键词
二氢杨梅素/人血清白蛋白/荧光猝灭/分子对接/相互作用Key words
dihydromyricetin/human serum albumin/fluorescence quenching/binding interaction/molecular docking分类
医药卫生引用本文复制引用
曹团武,张林均,时建伟,贺薇,黄露平,任婷..光谱法和分子对接研究二氢杨梅素与人血清白蛋白相互作用[J].天然产物研究与开发,2018,30(1):33-40,83,9.基金项目
重庆市教委科学技术研究项目(KJ15012010) （KJ15012010）
长江师范学院科研创新平台建设项目(2015XJPT01) （2015XJPT01）
