Characterization of the binding of chrysoidine, an illegal food additive to bovine serum albumin

被引：33

作者：

Yang, Bingjun ^{[1
]}

Hao, Fang ^{[1
]}

Li, Jiarong ^{[1
]}

Wei, Kai ^{[1
]}

Wang, Wenyu ^{[1
]}

Liu, Rutao ^{[1
]}

机构：

[1] Shandong Univ, Sch Environm Sci & Engn, China Amer CRC Environm & Hlth, Jinan 250100, Shandong, Peoples R China

来源：

FOOD AND CHEMICAL TOXICOLOGY | 2014年 / 65卷

关键词：

Proteins; Dyes; Spectroscopy; Isothermal titration calorimetry; Thermodynamics; Molecular docking; ENERGY-TRANSFER; EQUILIBRIUM; PROTEIN; DOMAIN; ALPHA; DYE;

D O I：

10.1016/j.fct.2013.12.047

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Chrysoidine is an industrial azo dye and the presence of chrysoidine in water and food has become an environmental concern due to its negative effects on human beings. Binding of dyes to serum albumins significantly influence their absorption, distribution, metabolism, and excretion properties. In this work, the interactions of chrysoidine with bovine serum albumin (BSA) were explored. Isothermal titration calorimetry results reveal the binding stoichiometry of chrysoidine to BSA is 1:15.5, and van der Waals and hydrogen bonding interactions are the major driving force in the binding of chrysoidine to BSA. Molecular docking simulations show that chrysoidine binds to BSA at a cavity close to Sudlow site I in domain IIA. However, no detectable conformational change of BSA occurs in the presence of chrysoidine as revealed by UV-vis absorption, circular dichroism and fluorescence spectroscopy studies. (C) 2014 Elsevier Ltd. All rights reserved.

引用

页码：227 / 232

页数：6

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