Study of the Interaction of Galangin, Kaempferol and Quercetin with Bsa

−− The interactions between Bovine Serum Albumin (BSA) and three flavonols, galangin, kaempferol and quercetin were studied by means of fluorescence spectroscopy. The fluorescence intensity of BSA exhibits remarkable decrease along with appreciable blue-shift of its maximum emission wavelength upon addition of the three compounds, respectively. The respective binding constant Kα and number of binding sites of each compound were calculated, and the quenching mechanism was proposed. Based on the values of thermodynamic parameters, the binding of each compound proceeds spontaneously with BSA. The binding distance between each and BSA was obtained by Foerster's dipole-dipole non-radiation energy transfer mechanism. Keywords−− Galangin, Kaempferol, Quercetin, flavonols, Bovine Serum Albumin, Fluorescence Spectroscopy.