Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin.
- Author:
Ji-cai FAN
1
;
Xiang CHEN
;
Yun WANG
;
Cheng-ping FAN
;
Zhi-cai SHANG
Author Information
1. Department of Chemistry, Zhejiang University, Hangzhou 310027, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Anti-Bacterial Agents;
chemistry;
metabolism;
pharmacology;
Binding Sites;
Cattle;
Humans;
Kinetics;
Lactoferrin;
chemistry;
metabolism;
Pefloxacin;
chemistry;
metabolism;
pharmacology;
Protein Binding;
Protein Conformation;
Serum Albumin;
chemistry;
metabolism;
Spectrometry, Fluorescence;
Spectrophotometry, Ultraviolet
- From:
Journal of Zhejiang University. Science. B
2006;7(6):452-458
- CountryChina
- Language:English
-
Abstract:
The binding of pefloxacin mesylate (PFLX) to bovine lactoferrin (BLf) and human serum albumin (HSA) in dilute aqueous solution was studied using fluorescence spectra and absorbance spectra. The binding constant K and the binding sites n were obtained by fluorescence quenching method. The binding distance r and energy-transfer efficiency E between pefloxacin mesylate and bovine lactoferrin as well as human serum albumin were also obtained according to the mechanism of Förster-type dipole-dipole nonradiative energy-transfer. The effects of pefloxacin mesylate on the conformations of bovine lactoferrin and human serum albumin were also analyzed using synchronous fluorescence spectroscopy.
