Binding of bezafibrate to human serum albumin: insight into the non-covalent interaction of an emerging contaminant with biomacromolecules.
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%.
Key Laboratory of Yangtze River Water Environment for Ministry of Education, College of Environmental Science and Engineering, Tongji University, Shanghai 200092, China.
Yajie
Y
Qian
Xuefei
X
Zhou
Jiabin
J
Chen
Yalei
Y
Zhang
D001629:Bezafibrate / Q000737:chemistry* / Q000378:metabolism; D004785:Environmental Pollutants / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D004785:Environmental Pollutants; D012709:Serum Albumin; D001629:Bezafibrate