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Comparative studies on the interaction of cefixime with bovine serum albumin by fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy
Author(s) -
Zhang Lihui,
Liu Baosheng,
Li Zhiyun,
Guo Ying
Publication year - 2015
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.2805
Subject(s) - cefixime , bovine serum albumin , quenching (fluorescence) , fluorescence , chemistry , fluorescence spectroscopy , spectroscopy , analytical chemistry (journal) , chromatography , biochemistry , optics , physics , quantum mechanics , cephalosporin , antibiotics
Under simulated physiological conditions, the reaction mechanism between cefixime and bovine serum albumin at different temperatures (293, 303 and 310 K) was investigated using a fluorescence quenching method and synchronous fluorescence method, respectively. The results indicated that the fluorescence intensity and synchronous fluorescence intensity of bovine serum albumin decreased regularly on the addition of cefixime. In addition, the quenching mechanism, binding constants, number of binding sites, type of interaction force and energy‐transfer parameters of cefixime with bovine serum albumin obtained from two methods using the same equation were consistent. The results indicated that the synchronous fluorescence spectrometry could be used to study the binding mechanism between drug and protein, and was a useful supplement to the conventional method. Copyright © 2014 John Wiley & Sons, Ltd.