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光谱法研究酸度对一种白杨素衍生物与牛血清白蛋白相互作用的影响
引用本文:于岚岚,陈晓英,张守仁,陈晓岚,杨冉,屈凌波.光谱法研究酸度对一种白杨素衍生物与牛血清白蛋白相互作用的影响[J].光谱实验室,2011,28(4):2120-2127.
作者姓名:于岚岚  陈晓英  张守仁  陈晓岚  杨冉  屈凌波
作者单位:1. 郑州大学化学系 郑州市科学大道100号450001
2. 郑州大学化学系 郑州市科学大道100号450001;河南工业大学化学化工学院 郑州市中原路195号450052
基金项目:国家自然科学基金,河南省杰出青年基金资助项目,教育部留学回国人员科研启动基金资助项目,中国博士后科学基金资助项目
摘    要:在3种酸度条件下,采用多种光谱技术对一种白杨素衍生物和牛血清白蛋白的相互作用进行了研究.结果表明该衍生物和牛血清白蛋白可形成基态复合物,静态、动态猝灭方式同时存在,以静态猝灭为主.通过计算获得了在不同温度及酸度条件下的结合常数及结合位点数.该衍生物在碱性条件下和牛血清白蛋白的结合能力较强.在pH 7.40的生理条件下,...

关 键 词:白杨素衍生物  牛血清白蛋白  荧光光谱法  同步荧光光谱  酸度

Spectroscopic Study on Effect of Acidity on Interaction Between a Chrysin Derivative and Bovine Serum Albumin
YU Lan-Lan,CHEN Xiao-Ying,ZHANG Shou-Ren,CHEN Xiao-Lan,YANG Ran,QU Ling-Bo.Spectroscopic Study on Effect of Acidity on Interaction Between a Chrysin Derivative and Bovine Serum Albumin[J].Chinese Journal of Spectroscopy Laboratory,2011,28(4):2120-2127.
Authors:YU Lan-Lan  CHEN Xiao-Ying  ZHANG Shou-Ren  CHEN Xiao-Lan  YANG Ran  QU Ling-Bo
Institution:a,ba(Department of Chemistry,Zhengzhou University,Zhengzhou 450001,P.R.China)b(College of Chemistry and Chemical Engineering,Industrial University of Henan,Zhengzhou 450052,P.R.China)
Abstract:The interaction between a chrysin derivative and bovine serum albumin was investigated by several spectroscopic techniques under three different acidity.The chrysin derivative formed ground state complex with bovine serum albumin.The possible mechanism of fluorescence quenching was the combination of static quenching and dynamic quenching,in which static quenching was predominant.The binding constant and number of binding site were obtained under different temperature and acidity by computing,and this chrysin derivative had stronger binding ability to bovine serum albumin in basic solution.Under the physiological condition at pH 7.40,the chrysin derivative exhibited stronger binding ability than chrysin.The hydrophobic interaction was the main force according to the thermodynamic parameters of combine for this chrysin derivative with bovine serum albumin.The distance between the chrysin derivative and bovine serum albumin was determined based on Foerster non-radiation energy transfer theory.The synchronous fluorescence spectra indicated that the chrysin derivative interacted with tryptophan and tyrosine residue in bovine serum albumin,and did not indicated bovine serum albumin effect with regional conformation in around bovine serum albumin.However the IR spectra indicated that the chrysin derivative induced the secondary structure change of bovine serum albumin.
Keywords:Chrysin Derivative  Bovine Serum Albumin  Fluorescence Spectroscopy  Synchronous Fluorescence Spectrum  Acidity
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