Studies on Interaction between Gatifloxacin and Bovine Serum Albumin by Spectroscopy

• 来源期刊: 中国化学（英文版）
• 年，卷（期）: 2007,（2）
• 页码范围: 182-185
• 页数: 4页
• 语种: 英文

摘要

The interaction of gatifloxacin (HGA) with bovine serum albumin (BSA) at 15 and 37 ℃ has been investigated by fluorescence quenching spectroscopy in aqueous solution. The bimolecular quenching rate constant was determined by Stem-Volmer curves and the values were Kq=9.28× 1012 L·mol-1·s-1 (15 ℃) and Kq=8.51 × 1012L·mol-1·s-1 (37 ℃). The results showed that the fluorescence quenching mechanism of BSA by HGA was a static quenching procedure. The thermodynamic parameters indicated that electrostatic forces played major role in the interaction of BSA with HGA. Studies on the relationship between the concentration of HGA and the fluorescence intensity of BSA showed that BSA and HGA bound at the molar ratio 1∶ 1 and the equilibrium constant K0 was 6.80× 104 L·mol 1. The binding distances between BSA and HGA and the energy transfer efficiency were obtained based on the F(o)rster's theory.