Modification on The Interaction Between Bovine Serum Albumin and Fluprofen by Improved Fluorescence Spectroscopy

In the Tris-HCl buffer solution which pH was 7. 40,the interaction of bovine serum albumin with fluprofen was investigated by classical fluorescence spectroscopy and improved fluorescence spectroscopy at 293,303 and 310 K,the conclusions of the two methods were consistent. The results showed that fluprofen could quench the intrinsic fluorescence of bovine serum albumin,and the quenching mechanism was a static quenching process. The static electricity forces attraction played an important role on the conjugation reaction between BSA and fluprofen,the number of binding site( n) in the binary system was approximately to 1. The values of Hill's coefficients were more than 1,which indicated very weakly positive cooperativity in bovine serum albumin-fluprofen system. The binding constant( K a) that obtained by improved fluorescence spectroscopy was much larger than the one obtained by classical fluorescence spectroscopy,which indicated that it was more accurate and reasonable when regarding the drug as the research object. At last,the scientificalness of the new method based on improved fluorescence spectroscopy was verified by ultraviolet spectroscopy.