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

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 x 10(8) l/mol. The thermodynamic parameters, with a negative value of Delta G(0), revealed that the binding is a spontaneous process. A binding distance R of 1.19 nm between donor and acceptor was obtained from the Forster energy transfer theory.