On the interaction between cefonicid sodium and bovine serum albumin by spectrometry / 安徽医科大学学报

ABSTRACT

Obiective To explore the interaction of cefonicid sodium(CS) with bovine serum albumin(BSA) by fluorescence and absorption spectroscopy. Methods The rate constant(Kq), quenching constant(Ksv), static fluo-rescence quenching association constant(KLB),binding site number(n) and binding constant(Kb) were calculated using Stern-Volmer, Lineweaver-Burk and double logarithm equations. Results CS was able to bind to BSA. The probable quenching mechanism of BSA by CS was mainly static quenching due to the formation of a CS-BSA com-plex. The results of thermodynamic parameters indicated that electrostatic force plays the main role in the binding process and the binding process was spontaneous. There was a single class of binding site for the BSA with CS. The primary binding site for CS was located at sub-domainⅡA of BSA and near by tyrosine residue. There was almost some negative cooperative effect. The results obtained from synchronous fluorescence showed that CS could change the microenvironment of Tyrand Trp residues of BSA. Conclusion The interaction between CS and BSA is dynam-ic. There is a single class of binding site for the BSA with CS. The obtained results provide references for its clini-cal application.