Investigation on the interaction of cefpirome sulfate with lysozyme by fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy. (24th August 2015)

• Record Type: Journal Article
• Authors: Han, Rong; Liu, Baosheng; Li, Gaixia; Zhang, Qiuju
• Is Part Of: Luminescence. Volume 31:Number 2(2016:Mar./Apr.)
• Page Start: 580
• Page End: 586
• Publication Date: 2015-08-24
• Subjects: fluorescence quenching spectroscopy -- synchronous fluorescence spectroscopy -- cefpirome sulfate -- lysozyme -- interaction; Luminescence -- Periodicals; Bioluminescence -- Periodicals; Chemiluminescence -- Periodicals; Luminescence -- Periodicals; 535.35
• DOI: 10.1002/bio.2998
• Languages: English
• ISSNs: 1522-7235

Abstract

Abstract: The reaction mechanism of cefpirome sulfate with lysozyme at different temperatures (298, 310 and 318 K) was investigated using fluorescence quenching and synchronous fluorescence spectroscopy under simulated physiological conditions. The results clearly demonstrated that cefpirome sulfate caused strong quenching of the fluorescence of lysozyme by a static quenching mechanism. The binding constants obtained using the above methods were of the same order of magnitude and very similar. Static electric forces played a key role in the interaction between cefpirome sulfate and lysozyme, and the number of binding sites in the interaction was close to 1. The values of Hill's coefficients were > 1, indicating that drugs or proteins showed a very weakly positive cooperativity in the system. In addition, the conclusions obtained from the two methods using the same equation were consistent. The results indicated that synchronous fluorescence spectrometry could be used to study the binding mechanism between drug and protein, and was a useful supplement to the fluorescence quenching method. In addition, the effect of cefpirome sulfate on the secondary structure of lysozyme was analyzed using circular dichroism spectroscopy. Copyright © 2015 John Wiley & Sons, Ltd.