Investigation on The Interaction between p-Coumaric Acid and Human Serum Albumin by Fluorescence and Surface Enhanced Raman Spectra

SHEN Bing-jun; JIN Li-hong; ZHANG Jia-jia; LIU Rong-juan; LIU Zhan-wei; LIU Yu-xin; CHAI H

doi:10.3788/fgxb20163710.1259

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Investigation on The Interaction between p-Coumaric Acid and Human Serum Albumin by Fluorescence and Surface Enhanced Raman Spectra

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- Investigation on The Interaction between p-Coumaric Acid and Human Serum Albumin by Fluorescence and Surface Enhanced Raman Spectra
- Chinese Journal of Luminescence Vol. 37, Issue 10, Pages: 1259-1266(2016)
- 作者机构：
  
  1. 长春理工大学清洁能源技术研究所,吉林长春,130022
  2. 长春理工大学生命科学技术学院,吉林长春,130022
- 作者简介：
- 基金信息：
- DOI：10.3788/fgxb20163710.1259
  CLC： O657.3
- Received：18 April 2016，
  
  Revised：04 August 2016，
  
  Published：05 October 2016
- 稿件说明：
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申炳俊, 金丽虹, 张佳佳等. 对-香豆酸与人血清白蛋白相互作用的荧光和表面增强拉曼光谱研究[J]. 发光学报, 2016,37(10): 1259-1266

SHEN Bing-jun, JIN Li-hong, ZHANG Jia-jia etc. Investigation on The Interaction between p-Coumaric Acid and Human Serum Albumin by Fluorescence and Surface Enhanced Raman Spectra[J]. Chinese Journal of Luminescence, 2016,37(10): 1259-1266
申炳俊, 金丽虹, 张佳佳等. 对-香豆酸与人血清白蛋白相互作用的荧光和表面增强拉曼光谱研究[J]. 发光学报, 2016,37(10): 1259-1266 DOI： 10.3788/fgxb20163710.1259.

SHEN Bing-jun, JIN Li-hong, ZHANG Jia-jia etc. Investigation on The Interaction between p-Coumaric Acid and Human Serum Albumin by Fluorescence and Surface Enhanced Raman Spectra[J]. Chinese Journal of Luminescence, 2016,37(10): 1259-1266 DOI： 10.3788/fgxb20163710.1259.

摘要

在模拟生理条件下，应用荧光光谱和表面增强拉曼光谱法对对-香豆酸（

-CA）与人血清白蛋白（HSA）的结合机理进行研究。结果表明，

-CA对HSA的荧光猝灭机制为静态猝灭，并伴有非辐射能量转移。荧光光谱显示，在298，304，310 K下，

-CA与HSA的结合常数（

）分别为3.4110

，2.0910

，1.3810

L/mol，结合位点数（

）近似为1。表面增强拉曼光谱研究揭示，

-CA的酚基与HSA有效结合。标记竞争实验指出，

-CA在HSA上的结合位点主要在SiteⅠ。反应过程热力学参数表明，二者间的作用主要为静电引力，且根据Frster能量转移理论求得

-CA与HSA间的距离为 5.11 nm。同步荧光光谱显示，

-CA的结合没有导致HSA构象发生明显变化。

Abstract

Under simulated physiological conditions

the binding mechanism between

-Coumaric acid (

-CA) and human serum albumin (HSA) was investigated by fluorescence spectrum and surface enhanced Raman scattering (SERS). The results show that the effect between

-CA and HSA is a static fluorescence quenching with Frster's non-radioactive energy transformation. At 298

304

310 K

the binding constants (

) between

-CA and HSA are 3.4110

2.0910

1.3810

L/mol

the binding site (

) value is approximate to 1. SERS reveals that the phenolic group of

-CA combines with HSA. Thermodynamic data indicate that the interaction between

-CA and HSA is mainly electrostatic attraction. Marker competition experiments point out that the primary binding site for

-CA is located at site Ⅰ in HSA. According to Frster energy transfer theory

the binding distance between

-CA and HSA is 5.11 nm. Synchronous fluorescence spectra show that the conformation of HSA does not changed apparently with the addition of

-CA.

关键词

Keywords

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