Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin

摘要

The interaction between fosfomycin(FOS) and bovine serum albumin(BSA) has been investigated effectively by multi-spectroscopic techniques under physiological p H 7.4. FOS quenched the intrinsic fl uorescence of BSA via static quenching. The number of binding sites n and observed binding constant K A were measured by the fl uorescence quenching method. The thermodynamic parameters ΔG0, ΔH0andΔS0were calculated at different temperatures according to the van't Hoff equation. The site of binding of FOS in the protein was proposed to be Sudlow's site I based on displacement experiments using site markers viz. warfarin, ibuprofen and digitoxin. The distance r between the donor(BSA) and acceptor(FOS) molecules was obtained according to the F?rster theory. The effect of FOS on the conformation of BSA was analyzed using synchronous fl uorescence spectra(SFS), circular dichroism(CD) and 3D fl uorescence spectra. A molecular modeling study further con fi rmed the binding mode obtained by the experimental studies.