Spectroscopic studies on the interaction of carteolol hydrochloride and urea-induced bovine serum albumin

The interaction between carteolol hydrochloride (CTL) and urea-induced bovine serum albumin was studied by fluorescence and UV-vis spectroscopy. The quenching mechanism, binding constants, and binding distance were determined. Conformation change of BSA was observed from synchronous fluorescence spectra. The comparison of binding potency of SPSD and BSA suggested that the temperature influence the binding affinity of CTL and urea-induced BSA.