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 ΔG°, ΔH° and ΔS° were calculated according to van't Hoff equation. The calculated distance r between FOS and the protein is evaluated according to the theory of Förster 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.
P. G. Department of Studies in Chemistry, Karnatak University, Pavate Nagar, Dharwad, 580003, India.
Manjunath D
MD
Meti
Kirthi S
KS
Byadagi
Sharanappa T
ST
Nandibewoor
Shrinivas D
SD
Joshi
Uttam A
UA
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Shivamurti A
SA
Chimatadar
D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D002942:Circular Dichroism; D005578:Fosfomycin / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D007477:Ions / Q000737:chemistry; D008968:Molecular Conformation; D062105:Molecular Docking Simulation; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013057:Spectrum Analysis; D013816:Thermodynamics
D000900:Anti-Bacterial Agents; D007477:Ions; D012709:Serum Albumin; D005578:Fosfomycin