In vitro studies on the interaction between human serum albumin and fosfomycin disodium salt, an antibiotic drug by multi-spectroscopic and molecular docking methods
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  • 作者:Manjunath D. Meti (1)
    Kirthi S. Byadagi (1)
    Sharanappa T. Nandibewoor (1)
    Shrinivas D. Joshi (2)
    Uttam A. More (2)
    Shivamurti A. Chimatadar (1)
  • 关键词:Fosfomycin ; Binding ; Spectroscopic methods ; Circular dichroism ; Fluorescence quenching ; Secondary structure
  • 刊名:Molecular Biology Reports
  • 出版年:2014
  • 出版时间:April 2014
  • 年:2014
  • 卷:41
  • 期:4
  • 页码:2377-2387
  • 全文大小:3,285 KB
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  • 作者单位:Manjunath D. Meti (1)
    Kirthi S. Byadagi (1)
    Sharanappa T. Nandibewoor (1)
    Shrinivas D. Joshi (2)
    Uttam A. More (2)
    Shivamurti A. Chimatadar (1)

    1. P. G. Department of Studies in Chemistry, Karnatak University, Pavate Nagar, Dharwad, 580003, India
    2. Novel Drug Design and Discovery Laboratory, Department of Pharmaceutical Chemistry, S.E.T’s College of Pharmacy, Sangolli Rayanna Nagar, Dharwad, 580002, Karnataka, India
  • ISSN:1573-4978
文摘
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 F?rster 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.

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