Study of the interaction between bovine serum albumin and analogs of Biphenyldicarboxylate by spectrofluorimetry

被引：36

作者：

Wang, Ruiyong ^{[1
]}

Chai, Yahui ^{[1
]}

Wang, Ruiqiang ^{[2
]}

Zhang, Lu ^{[1
]}

Wu, Jing ^{[1
]}

Chang, Junbiao ^{[1
]}

机构：

[1] Zhengzhou Univ, Dept Chem, Zhengzhou 450001, Peoples R China

[2] Zhengzhou Univ, Affiliated Hosp 1, Zhengzhou 450052, Peoples R China

来源：

SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY | 2012年 / 96卷

基金：

中国博士后科学基金; 中国国家自然科学基金;

关键词：

Fluorescence spectroscopy; Bovine serum albumin; Biphenyldicarboxylate; Analogs; FLUORESCENCE; BINDING; PROTEIN; OXYGEN; PROBE;

D O I：

10.1016/j.saa.2012.05.030

中图分类号：

O433 [光谱学];

学科分类号：

0703 ; 070302 ;

摘要：

This work was designed to study the interaction between bovine serum albumin (BSA) and Biphenyldicarboxylate (DDB) or analogs (I, II and III) of DDB by UV-visible and fluorescence spectroscopic methods for the first time. Results showed that both DDB and analogs had a strong ability to quench the intrinsic fluorescence of BSA through a static quenching procedure. The binding constants (K) were calculated according to the relevant fluorescence data. The thermodynamic parameters (Delta H, Delta S and Delta G) showed that the hydrophobic force played a major role in the binding interaction between BSA and DDB or analogs. Synchronous fluorescence spectra of BSA were investigated in the presence of DDB or analogs. It was showed that DDB was the strongest quencher and bound to BSA with the highest affinity among four compounds. The influence of molecular structure on the binding aspects was reported. (C) 2012 Elsevier B.V. All rights reserved.

引用

页码：324 / 331

页数：8

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