天然产物研究与开发 ›› 2018, Vol. 30 ›› Issue (1): 33-40.doi: 10.16333/j.1001-6880.2018.1.006

• 研究论文 • 上一篇    下一篇

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

曹团武*,张林均,时建伟,贺薇,黄露平,任婷   

  1. 长江师范学院化学化工学院 武陵山天然药物研究与开发实验室,重庆 408100
  • 出版日期:2018-01-26 发布日期:2018-01-30
  • 基金资助:

    重庆市教委科学技术研究项目(KJ15012010);长江师范学院科研创新平台建设项目(2015XJPT01)

The Interaction of Dihydromyricetin with Human Serum Albumin by Spectroscopic Methodologies and Molecular Docking

CAO Tuan-wu*, ZHANG Lin-jun, SHI Jian-wei, HE Wei, HUANG Lou-ping, REN Ting   

  1. Laboratory of Natural Medicine Research and Development in Wuling Mountain, School of Chemistry and Chemical Engineering,Yangtze Normal University, Chongqi Fuling 408100, China
  • Online:2018-01-26 Published:2018-01-30

摘要: 运用光谱法和分子对接理论研究了二氢杨梅素(dihydromyricetin,DMY)与人血清白蛋白(Human serum albumin,HSA)的相互作用。结果表明,DMY有规律的使HSA内源荧光猝灭,其猝灭机制为两者形成复合物而引起的的静态猝灭;两者结合常数KA均大于105 L/mol,结合位点数n接近于1。根据热力学参数判断,两者结合反应能自发进行,主要作用力类型为静电作用力。计算得到DMY与HSA的结合距离r为3.32 nm,表明两者结合过程发生了非辐射能量转移。同步荧光和三维光谱分析结果显示,DMY使HSA的构象发生了一定程度的改变。位点竞争实验和分子对接结果表明,DMY在HSA上的更倾向结合位于亚结构域IIA(Site I)。

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

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 Forster’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.

Key words: dihydromyricetin, human serum albumin, fluorescence quenching, binding interaction, molecular docking

中图分类号: 

R966