Interaction between Sodium Dodecylbenzene Sulfonate and Bovine Serum Albumin
Binding interaction between sodium dodecylbenzene sulfonate(SDBS)and bovine serum albumin(BSA)was studied by fluorescence and absorption spectroscopy in physiological conditions.Results showed that fluorescence of BSA was quenched by SDBS,and the quenching mechanism was static.Binding constants and thermodynamic parameters were obtained at different temperatures.Main binding force was hydrogen bonds and Van der waals.Results of synchronous fluorescence spectra indicated that conformation of BSA was changed and hydrophobicity near tryptophan residues were increased at the presence of SDBS.