Study on the interactions of PFOS and PFOA with bovine serum albumin

The interactions of PFOS and PFOA with bovine serum albumin were studied by fluorescence spectroscopy. It was observed that both of them can effectively quench the intrinsic fluorescence of BSA, the quench of BSA by PFOS is more effective than by PFOA. The dynamic quenching existed between PFOS/PFOA and BSA according to the flurescence quenching data at different temperatures and the UV. The results of thermodynamics indicate that the interactions of PFOS and PFOA with bovine serum albumin were spontaneous. The binding reaction between PFOS/PFOA and BSA were driven mainly by hydrophobic interaction. Synchronous spectra were obtained, which showed that the binding of PFOS and PFOA to BSA had strong impact on the Tryptophan residues.