Binding of bezafibrate to human serum albumin: Insight into the non-covalent interaction of an emerging contaminant with biomacromolecules

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 × 10 3, 2.84 × 10 3 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 a-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 B 2 to HSA by 29%. © 2012 by the authors.