Journal
FOOD AND CHEMICAL TOXICOLOGY
Volume 65, Issue -, Pages 227-232Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.fct.2013.12.047
Keywords
Proteins; Dyes; Spectroscopy; Isothermal titration calorimetry; Thermodynamics; Molecular docking
Categories
Funding
- NSFC [21277081]
- Ministry of Education of China [708058]
- Independent innovation program of Jinan [201202083]
- Independent innovation foundation of Shandong University natural science projects [2012DX002]
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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.
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