高等学校化学学报 ›› 2015, Vol. 36 ›› Issue (8): 1511-1516.doi: 10.7503/cjcu20150119

• 分析化学 • 上一篇    下一篇

荧光各向异性结合同步荧光法研究1-羟基芘与牛血清白蛋白的相互作用

张静1, 陈薇晓1,2, 张唯1, 段滢1, 朱玉秀1, 朱亚先3, 张勇1,4()   

  1. 1. 近海海洋环境科学国家重点实验室, 厦门大学环境与生态学院, 厦门 361102
    2. 北京大学城市与环境学院, 北京 100871
    3. 厦门大学化学化工学院化学系, 厦门 361005
    4. 漳州职业技术学院, 漳州 363000
  • 收稿日期:2015-02-02 出版日期:2015-08-10 发布日期:2015-06-30
  • 作者简介:联系人简介: 张 勇, 男, 博士, 教授, 博士生导师, 主要从事环境化学研究. E-mail:yzhang@xmu.edu.cn
  • 基金资助:
    国家自然科学基金(批准号: 21075102, 21177102)、 中央高校基本科研业务费专项资金(批准号: 2013121052)和国家级大学生创新创业项目基金(批准号: DC2013035)资助

Interaction of 1-Hydroxypyrene with BSA Using Fluorescence Anisotropy and Synchronous Fluorescence Analysis Methods

ZHANG Jing1, CHEN Weixiao1,2, ZHANG Wei1, DUAN Ying1, ZHU Yuxiu1, ZHU Yaxian3, ZHANG Yong1,4,*()   

  1. 1. State Key Laboratory of Marine Environmental Sciences of China, College of Environment and Ecology, Xiamen University, Xiamen 361102, China
    2. College of Urban and Environmental Sciences, Peking University, Beijing 100871, China
    3. College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China
    4. Zhangzhou Institute of Technology, Zhangzhou 363000, China
  • Received:2015-02-02 Online:2015-08-10 Published:2015-06-30
  • Contact: ZHANG Yong E-mail:yzhang@xmu.edu.cn
  • Supported by:
    † Supported by the National Natural Science Foundation of China(Nos.1075102, 21177102), the Fundamental Research Funds for the Central Universities, China(No.2013121052) and the National Training Program of Innovation and Enterpreneurship for Undergraduates, China(No;DC2013035)

摘要:

在模拟生理条件下, 应用荧光各向异性法研究了多环芳烃(PAHs)代谢标志物1-羟基芘(1-OHP)与牛血清白蛋白(BSA)的相互作用, 并结合同步荧光法研究作用过程中BSA的构型变化, 初步探讨了二者的结合方式. 研究结果表明, 1-OHP与BSA有较强的结合作用, 形成1∶1复合物, 平均结合平衡常数为3.63×106 L/mol, 且其结合作用强弱随着BSA浓度大小发生变化. 1-OHP可与BSA的色氨酸残基结合, 使BSA构型发生变化, 进而使色氨酸残基周围环境的疏水性降低.

关键词: 荧光各向异性, 1-羟基芘, 牛血清白蛋白, 结合常数, 构型变化, 作用方式

Abstract:

Fluorescence anisotropy was employed to investigate the interaction of 1-hydroxypyrene(1-OHP), the metabolism biomarker of PAHs in vivo, with a model transport protein of bovine serum albumin(BSA) under simulated physiological conditions. Combined with synchronous fluorescence spectra, the conformation transition of BSA was also investigated. The experiment results showed that 1-OHP can bind to BSA strongly and a 1∶1 complex was formed, with an average binding equilibrium constant of 3.63×106 L/mol. Also as the amounts of BSA differ, the interaction of 1-OHP and BSA was dominated by strong and weak binding modes alternately. Moreover, 1-OHP can bind to tryptophan residues and induce the conformational and micro-environmental changes of BSA, increasing the tryptophan residue of BSA exposuring to a less hydrophobic micro-environment.

Key words: Fluorescence anisotropy, 1-Hydroxypyrene(1-OHP), Bovine serum albumin(BSA), Binding constant, Conformation change, Interaction mode(Ed.: N, K)

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