Study on the Interaction Between Tropeolin G and Bovine Serum Albumin by Fluorescence Spectroscopy

The interaction between tropeolin G and bovine serum albumin(BSA)was investigated mainly by fluorescence spectroscopy.Tropeolin G can remarkably quench the fluorescence intensity of BSA,and the fluorescence quenching effect is a static quenching process with forming the supramolecular complex.The binding constants and thermodynamic parameters of interaction between tropeolin G and bovine serum albumin were studied.Basing on the theory of Ross,the main sort of binding force between tropeolin G and BSA were attributed to static-electricity gravitation,which was conformed by the calculation results of thermodynamic parameters of this process.The binding distance between tropeolin G and BSA was obtained according to Foerster's nonradioactive energy transfer theory.