Spectroscopic Investigation of the Interaction Between Gemini Surfactant and Bovine Serum Albumin

In this paper,a fluorescence method was used to study at different temperature the fluorescence quenching of bovine serum albumin(BSA) by its interaction with Gemini 14-3-14(G14-3-14).The analysis of fluorescence data indicated the presence of dynamic quenching mechanism in the binding.The interaction association constants of BSA and G14-3-14 were determined from a double reciprocal line Weaver-Burk plot.Fluorescence quenching constants between G14-3-14 and BSA were obtained at 303K and 308K.Fluorescence data showed that quenching constants would be higher with increasing temperature which could induce the fluorescence quenching of BSA by dynamic quenching.According to Stern-Volmer equation,the binding constants at different temperatures were 1.01×105 L·mol-1,5.45×106 L·mol-1 and the binding numbers were 0.9978,0.9977.The enthalpy change(△H) and entropy change(ΔS) were calculated to be 32.65 KJ·mol-1,and 203.56 J·mol-1·K-1(303K).From the spectral results it can be judged that the binding power between G14-3-14 and BSA is hydrophobic effect.