Spectroscopic study of the interaction between flucythrinate and bovine serum albumin

The interaction of flucythrinate(FC) and bovine serum albumin(BSA) under physiological condition was investigated by spectroscopic methods and the quenching constants at different temperatures were measured.The fluorescence results revealed that FC caused the fluorescence quenching of BSA through a static quenching procedure at low concentrations.Thermodynamic parameters ΔG,ΔH and ΔS at different temperatures were calculated.The data indicated that the van der Waals force was the dominant intermolecular force in stabilizing the complex and the binding process was spontaneous.In addition,the impact of FC on the conformation of BSA was analyzed using synchronous fluorescence and circular dichroism spectroscopy.The CD spectra results showed that the α-helix content of BSA decreased.It's concluded that the microenvironment and conformation of BSA were changed in the binding reaction.