Acta Phys. -Chim. Sin. ›› 2005, Vol. 21 ›› Issue (02): 123-127.doi: 10.3866/PKU.WHXB20050203

• ARTICLE • Previous Articles     Next Articles

The Binding Mode of Pefloxacin Mesylate with Human Serum Albumin

MA Guo-Zheng; TAN Fei; JIANG Yong-Jun; ZHENG Ke-Wen; GUO Ming; YU Qing-Sen   

  1. Department of Chemistry, Zhejiang University, Hangzhou　310027;　Key Laboratory for Molecular Design and Nutrition Engineering of Ningbo City, Ningbo Institute of Technology, Zhejiang University, Ningbo　315100
  • Received:2004-06-08 Revised:2004-08-17 Published:2005-02-15
  • Contact: JIANG Yong-Jun E-mail:yjjiang@nit.net.cn

PDF

3305

Like

Abstract: This study was designed to explore the binding mode of pefloxacin mesylate(PFLX) with human serum albumin (HSA).Fluorescence spectroscopic results showed pefloxacin-HSA complex with binding constants of 1.7×105 L•mol－1.The enthalpy change (ΔrHm) and entropy change (ΔrSm) were measured by microcalorimetry to be 1.03 kJ•mol－1 and 101.28 J•K－1•mol－1,which indicated that hydrophobic interaction played a major role in the binding of PFLX with HSA. The possible binding domains of HSA for PFLX were studied by molecular modeling, which predicted that the hydrophobic interaction played a dominating role in this drug-protein interaction and PFLX could bind to Sudlow’s sites I and II of HSA. The binding energies obtained from the molecular modeling were in accordance with the experiment results.

Key words: Pefloxacin mesylate, Human serum albumin, Molecular modeling, 　Binding mode