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Studies on Interaction between Gatifloxacin and Bovine Serum Albumin by Spectroscopy
Author(s) -
Liu XiaoHui,
Ye Yan,
Zeng ZhengZhi
Publication year - 2007
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200790037
Subject(s) - chemistry , bovine serum albumin , quenching (fluorescence) , binding constant , fluorescence , fluorescence spectroscopy , analytical chemistry (journal) , spectroscopy , aqueous solution , hydrophobic effect , chromatography , binding site , organic chemistry , biochemistry , physics , quantum mechanics
The interaction of gatifloxacin (HGA) with bovine serum albumin (BSA) at 15 and 37 °C has been investigated by fluorescence quenching spectroscopy in aqueous solution. The bimolecular quenching rate constant was determined by Stern‐Volmer curves and the values were K q =9.28×10 12 L·mol −1 ·s −1 (15 °C) and K q =8.51×10 12 L·mol −1 ·s −1 (37 °C). 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 K 0 was 6.80×10 4 L·mol −1 . The binding distances between BSA and HGA and the energy transfer efficiency were obtained based on the FÖrster's theory.