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
Chrysoidine is an industrial azo dye and the presence of chrysoidine in water and food has become anenvironmental concern due to its negative effects on human beings. Binding of dyes to serum albuminssignificantly influence their absorption, distribution, metabolism, and excretion properties. In this work,the interactions of chrysoidine with bovine serum albumin (BSA) were explored. Isothermal titrationcalorimetry results reveal the binding stoichiometry of chrysoidine to BSA is 1:15.5, and van der Waalsand 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 indomain IIA. However, no detectable conformational change of BSA occurs in the presence of chrysoidineas revealed by UV–vis absorption, circular dichroism and fluorescence spectroscopy studies
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