Abstract
In recent years, bezafibrate (BZF) has been frequently detected in environmental media. In order to reveal the toxicity of such an emerging pollutant, its interaction with human serum albumin (HSA) was studied by fluorescence spectrometry, circular dichroism, and equilibrium dialysis. Fluorescence data showed that the fluorescence quenching of HSA by BZF resulted from the formation of HSA-BZF complex. The binding constants were determined to be 3.33 × 103, 2.84 × 103 M−1 at 298 and 309.5 K, respectively. The thermodynamic determination indicated that the hydrophobic and electrostatic interaction were the dominant binding force. The conformational investigation showed that the presence of BZF increased the α-helix content of HSA and induced the slight unfolding of the polypeptides of protein. Finally, the equilibrium dialysis showed that 0.56 mM BZF decreased the binding of vitamin B2 to HSA by 29%.
Highlights
The occurrence and fate of pharmaceuticals and personal care products (PPCPs) in the environment have become a major cause for concern due to their potential toxic effect on the ecosystem and public health [1,2,3]
BZF is negatively charged in the neutral condition, so it would be first attracted around the alkaline amino residues of human serum albumin (HSA) by electrostatic attraction, the BZF molecule entered the hydrophobic pocket of HSA and the hydrophobic benzene ring reacted with the non-polar amino acid residues
The interaction between BZF and HSA was characterized by fluorescence spectrometry, circular dichroism (CD) and equilibrium dialysis
Summary
The occurrence and fate of pharmaceuticals and personal care products (PPCPs) in the environment have become a major cause for concern due to their potential toxic effect on the ecosystem and public health [1,2,3]. Human serum albumin (HSA) is the most abundant protein in blood plasma, which has a number of physiological functions involving transport of various endogenous and exogenous chemicals, e.g., pharmaceuticals. The distribution, metabolism, and toxicity of such chemicals are significantly affected by their binding to HSA. There is evidence of secondary structural change of HSA induced by its interaction with exogenous chemicals which will affect the physiological function of HSA [14]. Compared with other analytical techniques, fluorescence spectrometry is a conventional and powerful method to study the molecular interactions involving proteins, owing to its sensitivity, rapidity and simpleness. Great attempts were made to investigate the binding constant and site, the binding forces, and the effect of BZF on the conformational change, and subsequent physiological function of HSA
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