Investigation of the interaction between endocrine disruptor bisphenol A and human serum albumin.
In this study, the interaction of the endocrine disruptor bisphenol A (BPA) and human serum albumin (HSA) was investigated by molecular modelling, fluorescence, ultraviolet-visible spectroscopy (UV-vis), Fourier transform infrared spectroscopy (FT-IR) and circular dichroism spectroscopy (CD). The association constants between BPA and HSA were determined using the Scatchard equation. The thermodynamic parameters of the binding reaction (DeltaG0, DeltaH0 and DeltaS0) were measured, and they indicated the presence of hydrophobic forces in the BPA-HSA interaction, which agreed well with the results from molecular modelling. The alterations of protein secondary structure in the presence of BPA were confirmed by UV-vis, FT-IR and CD spectroscopy. Lastly, the average binding distance, r, between BPA and HSA was evaluated and found to be 1.82 nm according to Förster's theory of non-radiation energy transfer.
National Key Laboratory of Organic Chemistry, Department of Chemistry, Lanzhou University, Lanzhou 730000, China.
Xiaoyun
X
Xie
Xiaoru
X
Wang
Xiangmei
X
Xu
Huijun
H
Sun
Xingguo
X
Chen
D001559:Benzhydryl Compounds; D002942:Circular Dichroism; D004735:Energy Transfer; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D010636:Phenols / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics; D000098826:Bisphenol A Compounds
D001559:Benzhydryl Compounds; D010636:Phenols; D012709:Serum Albumin; C006780:bisphenol A; D000098826:Bisphenol A Compounds