National Key Laboratory of Organic Chemistry, Department of Chemistry, Lanzhou University, Lanzhou 730000, China.
Chemosphere. 2010 Aug;80(9):1075-80. doi: 10.1016/j.chemosphere.2010.04.076. Epub 2010 May 26.
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.
在这项研究中，通过分子建模、荧光、紫外可见光谱（UV-vis）、傅里叶变换红外光谱（FT-IR）和圆二色光谱（CD）研究了内分泌干扰物双酚 A（BPA）与人血清白蛋白（HSA）的相互作用。使用 Scatchard 方程确定了 BPA 与 HSA 之间的结合常数。测量了结合反应的热力学参数（ΔG0、ΔH0 和 ΔS0），结果表明 BPA-HSA 相互作用中存在疏水作用力，这与分子建模的结果一致。通过 UV-vis、FT-IR 和 CD 光谱证实了 BPA 存在时蛋白质二级结构的变化。最后，根据福斯特非辐射能量转移理论，评估了 BPA 与 HSA 之间的平均结合距离 r，结果为 1.82nm。
