光谱探针猩红S与牛血清白蛋白结合的发光光谱

刘保生; 薛春丽; 王晶; 杨超; 吕运开

doi:10.3788/fgxb20113201.0100

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光谱探针猩红S与牛血清白蛋白结合的发光光谱

光谱分析 | 更新时间：2020-08-12

- 光谱探针猩红S与牛血清白蛋白结合的发光光谱
- Luminescence Spectroscopy of Conjugation Reaction between Bovine Serum Albumin and Spectroscopic Probe Ponceau S
- 发光学报 2011年32卷第1期页码：100-107
- 作者机构：
  
  河北大学理化分析中心药物化学与分子诊断教育部重点实验室, 河北保定 071002
- 作者简介：
- 基金信息：
  
  Project supported by National Science Foundation of China (20675024)()
- DOI：10.3788/fgxb20113201.0100
  中图分类号： O657.3;O482.31
- 收稿日期：2010-10-25，
  
  修回日期：2010-11-15，
  
  网络出版日期：2011-01-22，
  
  纸质出版日期：2011-01-22
- 稿件说明：
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刘保生, 薛春丽, 王晶, 杨超, 吕运开. 光谱探针猩红S与牛血清白蛋白结合的发光光谱[J]. 发光学报, 2011,32(1): 100-107

LIU Bao-sheng, XUE Chun-li, WANG Jing, YANG Chao, LU Yun-kai. Luminescence Spectroscopy of Conjugation Reaction between Bovine Serum Albumin and Spectroscopic Probe Ponceau S[J]. Chinese Journal of Luminescence, 2011,32(1): 100-107
刘保生, 薛春丽, 王晶, 杨超, 吕运开. 光谱探针猩红S与牛血清白蛋白结合的发光光谱[J]. 发光学报, 2011,32(1): 100-107 DOI： 10.3788/fgxb20113201.0100.

LIU Bao-sheng, XUE Chun-li, WANG Jing, YANG Chao, LU Yun-kai. Luminescence Spectroscopy of Conjugation Reaction between Bovine Serum Albumin and Spectroscopic Probe Ponceau S[J]. Chinese Journal of Luminescence, 2011,32(1): 100-107 DOI： 10.3788/fgxb20113201.0100.

摘要

利用荧光光谱和紫外吸收光谱

详细研究了不同温度下猩红S (PS) 与牛血清白蛋白(BSA)的结合反应

发现PS对BSA的内源性荧光具有较强的猝灭作用

其猝灭机理属于静态猝灭

由此求得PS与BSA间的结合常数、结合位点数及热力学参数等。结果表明:PS与BSA之间形成了1 ∶ 1稳定复合物

它们之间的作用力主要是静电引力。根据Frster非辐射能量转移理论

确定了PS与BSA之间的结合距离

＜7 nm。同步荧光光谱研究表明:PS对BSA构象发生了影响

使BSA酪氨酸残基所处环境的极性减弱疏水性增强而色氨酸残基不受影响。利用对血清蛋白具有特异性结合的竞争试剂确定了PS在BSA 的键合位点为IIA亚区的site I

证明PS与BSA也存在特异性结合

PS可以用作新的位置探针替代竞争试剂来研究小分子与蛋白的结合位置。

Abstract

Ponceau S (PS) can quench the fluorescence of bovine serum albumin (BSA) in the aqueous solution of pH=7.40. The static fluorescence quenching process between BSA and PS was confirmed and the binding constant

the number of binding sites and thermodynamic parameters between BSA and PS were obtained. It showed that the number of binding sites was 1 and the electrostatic attraction played an important role in the binding of BSA to PS. Based on the theory of Frester energy transfer

the binding distance (

＜7.0 nm) between PS and BSA was obtained. Studies utilizing synchronous spectra showed that the conjugation reaction between PS and BSA would affect the conformation of BSA

leading to the weak polarity around tyrosine residues and the strong hydrophobicity. The site markers competitive experiments indicated that the binding of PS to BSA primarily took place in sub-domain ⅡA (site Ⅰ).

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references

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