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

ABSTRACT: The interaction between fosfomycin (FOS) and bovine serum albumin (BSA) has been investigated effectively by multi-spectroscopic techniques under physiological pH 7.4. FOS quenched the intrinsic fluorescence of BSA via static quenching. The number of binding sites n and observed binding constant K_A were measured by the fluorescence quenching method. The thermodynamic parameters ΔG⁰, ΔH⁰ and ΔS⁰ were 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) molecule

SUBMITTER: Meti MD 

PROVIDER: S-EPMC5762212 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature