Study on the Interaction of Bisphenol A and Bovine Serum Albumin by Spectroscopy

The toxic interaction of bisphenol A(BPA) with bovine serum albumin(BSA) was studied by using ?uorescence spectra and UV-vis absorption spectra.The experimental results indicate that the intrinsic fluorescence of BSA can be quenched by the addition of bisphenol A.The quenching mechanism is due to static quenching,and the binding constant is 2.54161×103,and the number of binding sites is 0.655931.The experimental results also show that the binding of bisphenol A to BSA can induce conformational changes to BSA,as shown by the UV–vis spectra.Such conformation changes can induce toxic effects.