Interaction of Decabromodiphenyl Ether with Bovine Serum Albumin by Fluorescence Spectroscopy

The interaction between decabromodiphenyl ether (Deca-BDE) and bovine serum albumin (BSA) in physiological buffer was studied by fluorescence quenching technique. Results showed that Deca-BDE has strong quenching function for the intrinsic fluorescence of BSA through a static quenching procedure. The binding constants (K) of Deca-BDE with BSA obtained by fluorescence quenching method were calculated to be 1.92 x 10(5), 1.97 x 10(5) and 2.16 x 10(5) L/mol at 277, 298 and 310 K, respectively. The binding sites of Deca-BDE on BSA had two and both were near tryptophan sites. Thermodynamic parameters obtained from data at different temperatures showed that the binding of Deca-BDE to BSA involved hydrophobic bonds predominantly. The result of synchronous fluorescence spectra showed that binding of Deca-BDE with BSA could induce conformational changes in BSA.