Spectroscopic Studies on the Interaction of Carteolol Hydrochloride and Urea-induced Bovine Serum Albumin

The interaction of carteolol hydrochloride, to 0.2 mol L(-1) urea-induced bovine serum albumin in aqueous solution has been first investigated by fluorescence spectra and ultraviolet-visible (UV-vis) spectra at pH 7.40. The quenching mechanism, binding parameter and sites (n), the binding mode (ΔG, ΔH, and ΔS) as well as the binding distance (r) have been obtained according to the experimental results. We also use the synchronous fluorescence method to study the effect of CTL on the conformation change of urea-induced BSA.