贝诺酯与牛血清白蛋白位点选择性结合的分子光谱研究

张彦峥; 陈芳; 王亚丹; 张银堂; 黄菊; 陈妍; 冶保献; 徐茂田

doi:10.3788/fgxb20123305.0562

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贝诺酯与牛血清白蛋白位点选择性结合的分子光谱研究

光谱分析 | 更新时间：2020-08-12

- 贝诺酯与牛血清白蛋白位点选择性结合的分子光谱研究
- Molecular Spectroscopic Study on Site-selective Binding of Benorilate to Bovine Serum Albumin
- 发光学报 2012年33卷第5期页码：562-570
- 作者机构：
  
  1. 郑州大学化学与分子工程学院, 河南郑州 450001
  2. 商丘师范学院化学化工学院, 纳米生物分析化学河南省高校重点实验室培育基地, 河南商丘 476000
- 作者简介：
- 基金信息：
  
  国家自然科学基金(20905045,21175091)();河南省科技攻关计划(102102310385,112102310217)();河南省教育厅自然科学基金(20
- DOI：10.3788/fgxb20123305.0562
  中图分类号： O657.3
- 纸质出版日期：2012-5-10，
  
  网络出版日期：2012-5-10，
  
  收稿日期：2012-2-20，
  
  修回日期：2012-3-26，
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张彦峥, 陈芳, 王亚丹, 张银堂, 黄菊, 陈妍, 冶保献, 徐茂田. 贝诺酯与牛血清白蛋白位点选择性结合的分子光谱研究[J]. 发光学报, 2012,(5): 562-570

ZHANG Yan-zheng, CHEN Fang, WANG Ya-dan, ZHANG Yin-tang, HUANG Ju, CHEN Yan, YE Bao-xian, XU Mao-tian. Molecular Spectroscopic Study on Site-selective Binding of Benorilate to Bovine Serum Albumin[J]. Chinese Journal of Luminescence, 2012,(5): 562-570
张彦峥, 陈芳, 王亚丹, 张银堂, 黄菊, 陈妍, 冶保献, 徐茂田. 贝诺酯与牛血清白蛋白位点选择性结合的分子光谱研究[J]. 发光学报, 2012,(5): 562-570 DOI： 10.3788/fgxb20123305.0562.

ZHANG Yan-zheng, CHEN Fang, WANG Ya-dan, ZHANG Yin-tang, HUANG Ju, CHEN Yan, YE Bao-xian, XU Mao-tian. Molecular Spectroscopic Study on Site-selective Binding of Benorilate to Bovine Serum Albumin[J]. Chinese Journal of Luminescence, 2012,(5): 562-570 DOI： 10.3788/fgxb20123305.0562.

摘要

采用荧光光谱、紫外可见光谱、同步荧光光谱及三维荧光光谱等分子光谱方法

研究了生理条件下贝诺酯(BEN)与牛血清白蛋白(BSA)的相互作用。结果表明

BEN对BSA的内源荧光有显著的猝灭作用

猝灭机理为动态猝灭

二者之间的作用力类型以疏水作用为主

BEN与BSA发生反应后

使BSA的疏水环境极性增强

疏水性减弱

荧光强度降低。测得的表观结合常数和结合位点数分别是1 050 Lmol

-1

和0.88

同时测得了焓变(

)、熵变(

)和自由能变(

)等热力学参数。同步荧光和三维荧光光谱的结果表明

BEN使BSA的构象发生改变。利用荧光特异性位点探针DA和DP

通过竞争结合实验

监测BEN与BSA的结合位点

测得了位点Ⅰ和位点Ⅱ的表观结合常数分别为4 300 Lmol

-1

和21 200 Lmol

-1

表明BEN与BSA优先在位点Ⅱ结合。

Abstract

The interaction between benorilate (BEN) and bovine serum albumin (BSA) was investigated under physiological condition by molecular spectroscopic techniques

including fluorescence spectroscopy

UV-visible spectroscopy

synchronous fluorescence spectroscopy and three-dimensional fluorescence spectroscopy. The intrinsic fluorescence of tryptophan in BSA was significantly quenched by BEN via dynamic quenching. The hydrophobic interaction did favor the interaction of BSA with BEN. The apparent binding constants and binding sites number at the tryptophan site were 1 050 Lmol

-1

and 0.88

respectively. Thermodynamic parameters such as enthalpy change (

)

entropy change (

) and free energy change (

) were also obtained. The conformation changes of BSA in the presence of BEN were proved by the evidences of synchronous fluorescence spectroscopy and three-dimensional fluorescence spectroscopy. Two site-specific fluorescence probes

dansylamide (DA) and dansyl-L-proline (DP)

were employed in competitive binding experiments to monitor the BEN binding sites of BSA. The apparent binding constants at siteⅠand Ⅱ were 4 300 and 21 200 Lmol

-1

respectively.

关键词

贝诺酯牛血清白蛋白荧光猝灭热力学参数三维荧光光谱

Keywords

benorilatebovine serum albuminfluorescence quenchingthermodynamic parametersthree-dimensional fluorescence spectroscopy

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