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光谱法研究槲皮苷与人血清白蛋白的相互作用
引用本文:黄芸,崔力剑,王建明,陈晨,窦玉红,韩冬.光谱法研究槲皮苷与人血清白蛋白的相互作用[J].中草药,2011,42(4):676-679.
作者姓名:黄芸  崔力剑  王建明  陈晨  窦玉红  韩冬
作者单位:1. 河北医科大学药学院,天然药物学教研室,河北,石家庄,050017
2. 河北医科大学中医学院,中药药理教研室,河北,石家庄,050091
基金项目:中国博士后科学基金面上项目,河北省自然科学基金项目
摘    要:目的研究槲皮苷与人血清白蛋白(HSA)的相互作用,并探讨葡萄糖对二者结合的影响。方法应用光谱法研究槲皮苷与HSA的作用机制,以双对数方程和能量转移原理计算槲皮苷与HSA的结合常数、结合位点数和结合距离;根据热力学参数判断二者的作用力类型;用同步荧光光谱考察槲皮苷对HSA构象的影响;观察葡萄糖浓度对反应结合常数和结合位点数的影响。结果槲皮苷对HSA的荧光猝灭过程为生成复合物的静态猝灭;结合常数和结合位点数随温度的升高而降低;结合距离小于7 nm;二者主要以疏水作用力相结合;槲皮苷与HSA的相互作用改变了色氨酸残基所处的微环境;葡萄糖的加入使结合常数和结合位点数均增加。结论槲皮苷能与HSA结合并改变HSA的构象,生理浓度的葡萄糖可增加槲皮苷与HSA的结合常数和结合位点数。

关 键 词:槲皮苷  人血清白蛋白(HSA)  荧光猝灭  同步荧光光谱  葡萄糖
收稿时间:7/2/2010 12:00:00 AM

Spectroscopic study on interaction of quercitrin with human serum albumin
HUANG Yun,CUI Li-jian,WANG Jian-ming,CHEN Chen,DOU Yu-hong and HAN Dong.Spectroscopic study on interaction of quercitrin with human serum albumin[J].Chinese Traditional and Herbal Drugs,2011,42(4):676-679.
Authors:HUANG Yun  CUI Li-jian  WANG Jian-ming  CHEN Chen  DOU Yu-hong and HAN Dong
Institution:HUANG Yun1,CUI Li-jian2,WANG Jian-ming1,CHEN Chen1,DOU Yu-hong2,HAN Dong1 1.Department of Natural Medicine,School of Pharmacy,Hebei Medical University,Shijiazhuang 050017,China 2.Department of Chinese Medicine Pharmacology,School of Traditional Chinese Medicine,Shijiazhuang 050091,China
Abstract:Objective To study the interaction of quercitrin with human serum albumin (HSA) and the influence of glucose. Methods To investigate the interaction mechanism between quercitrin and HSA by spectroscopic method; to calculate the binding constants,binding sites, and binding distance according to double logarithmic plot and Fosters energy transfer theory, respectively; to explain the type of interaction force between quercitrin with HSA by thermodynamic parameters; to discuss the conformation change of HSA via synchronous fluorescence spectra. Results The fluorescence quenching mechanism of quercitrin to HSA was static quenching; The binding constants and the number of binding sites decreased with the increasing of temperature and glucose; The distance between the donor and acceptor was less than 7 nm; The hydrophobic forces played a major role in stabilizing quercetrin and HSA complex; The binding reaction had changed the micro-environmention of tryptophan residues. Conclusion Quercetrin could bind with HSA and change the conformation of HSA; The physiological concentration of glucose increases the binding constants and the number of binding sites of quercetrin with HSA.
Keywords:quercetrin  human serum albumin(HSA)  fluorescence quenching  synchronous fluorescence spectra  glucose  
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