Spectroscopic investigations on the interaction of bovine serum albumin with amoxicillin and cloxacillin

The mechanism of interaction of two drugs viz., amoxicillin and cloxacillin with bovine serum albumin has been investigated using fluorescence absorption and circular dichroism spectroscopy. The quenching mechanism of fluorescence of bovine serum albumin by amoxicillin and cloxacillin was discussed. The binding sites number n and apparent binding constant Kwere measured by fluorescence quenching method. The thermodynamic parameters obtained from data at different temperatures were calculated. The distance r between donor (bovine serum albumin) and acceptor (amoxicillin and cloxacillin) was obtained according to Forster theory of non-radiative energy transfer. The effect of common ions on binding constant was also investigated. The results of synchronous fluorescence spectra, UV-vis absorption spectra and circular dichroism of BSA in presence of amoxicillin and cloxacillin show that the conformation of bovine serum albumin changed