In vitro studies on the interaction between human serum albumin and fosfomycin disodium salt, an antibiotic drug by multi-spectroscopic and molecular docking methods

The interaction between the human serum albumin (HSA) and drug, fosfomycin disodium salt (FOS) has been studied by different spectroscopic techniques. The experimental results showed a static quenching mechanism in the interaction of FOS with HSA. The number of binding sites, n and observed binding constant K (a) were measured by fluorescence quenching method. The thermodynamic parameters Delta GA degrees, Delta HA degrees and Delta SA degrees were calculated according to van't Hoff equation. The calculated distance r between FOS and the protein is evaluated according to the theory of Forster energy transfer. A change in the secondary structure of the protein was evident from the circular dichroism measurements, synchronous fluorescence and three-dimensional fluorescence spectra.