Fluorescence Spectrometric Study on the Interactions of Terazosin Hydrochloride and Prazosin Hydrochloride with Bovine Serum Albumin Using Warfarin and Diazepam as Site Markers

Abstract

The binding interaction of the terazosin hydrochloride and prazosin hydrochloride with bovine serum albumin (BSA) was studied by spectrofluorimetry. Both of these two compounds quenched the fluorescence of BSA. The thermodynamic parameters (ΔH ⁰, ΔS ⁰ and ΔG ⁰) obtained from the fluorescence data measured at two different temperatures showed that the binding of terazosin hydrochloride to BSA involved hydrogen bonds and that of prazosin hydrochloride to BSA involved hydrophobic and electrostatic interactions. In this work, the competitive interaction of the terazosin hydrochloride and prazosin hydrochloride with BSA was studied by three-way excitation-emission fluorescence with the aid of parallel factor analysis (PARAFAC).