Abstract

Investigation of the interaction between cefoxitin sodium and bovine serum albumin by improved spectroscopy

Author(s): Gaixia Li, Baosheng Liu, Rong Han, Qiuju Zhang

The reaction mechanism of cefoxitin sodium with bovine serum albumin was investigated using the classical fluorescence spectroscopy with focus on the fluorescence change of protein, as well as the elastic scattering fluorescence spectroscopy with focus on the fluorescence change of drug at different temperatures. The results indicated that cefoxitin sodium could quench the intrinsic fluorescence of bovine serum albumin strongly by a static quenching process. The results of two methods were consistent. In addition, the binding constant obtained from elastic scattering fluorescence spectroscopy was larger than the one obtained from classical fluorescence spectroscopy. At last the correctness of elastic scattering fluorescence spectroscopy method was verified by UVvisible absorption spectroscopy. It is also speculated that “point to surface ” interaction between drugs and peptides was existed.


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