Investigation on the Interaction of Prulifloxacin with Human Serum Albumin: A Spectroscopic Analysis

Abstract

The interaction between prulifloxacin (PUFX) and human serum albumin (HSA) was investigated under simulated physiologic conditions with fluorescence spectra. The fluorescence quenching process of HSA may be mainly governed by a static quenching mechanism. The apparent binding constant K_b between PUFX and HSA at different temperatures were 2.08±1.04, 2.74±0.50, and 4.98±1.61×10⁸ l/mol. The thermodynamic parameters, with a negative value of ΔG⁰, revealed that the binding is a spontaneous process. A binding distance R of 1.19 nm between donor and acceptor was obtained from the Fŏrster energy transfer theory.