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The study on interactions between levofloxacin and model proteins by using multi-spectroscopic and molecular docking

Qing Fang1, Chenhui Guo1, Yirun Wang1

  • 1a College of Life and Environmental Sciences, Minzu University of China , Beijing 100081 , China.

Journal of Biomolecular Structure & Dynamics
|June 13, 2017
PubMed
Summary

Levofloxacin (LEV) interacts with lysozyme, trypsin, and bovine hemoglobin, altering their structures and activities. These interactions are driven by hydrophobic forces, hydrogen bonds, and van der Waals forces, with LEV binding to active sites.

Keywords:
levofloxacinmodel proteinsmolecular dockingmulti-spectral techniques

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Molecular Biophysics

Background:

  • Levofloxacin (LEV) is a widely used antibiotic.
  • Understanding drug-protein interactions is crucial for drug development and predicting potential side effects.
  • Lysozyme (LYZ), trypsin, and bovine hemoglobin (BHb) are important model proteins for studying drug interactions.

Purpose of the Study:

  • To investigate the in vitro interactions between levofloxacin (LEV) and lysozyme (LYZ), trypsin, and bovine hemoglobin (BHb).
  • To elucidate the binding mechanisms, thermodynamic parameters, and structural changes induced by LEV binding to these proteins.
  • To determine the effect of LEV on the enzymatic activities of LYZ and trypsin.

Main Methods:

  • Multi-spectral techniques including fluorescence spectroscopy, UV-vis spectroscopy, and circular dichroism (CD) spectroscopy.
  • Molecular docking simulations.
  • Enzyme activity assays.

Main Results:

  • LEV exhibited static quenching with BHb and combined quenching with LYZ and trypsin, with varying binding constants.
  • Thermodynamic analysis indicated that hydrophobic forces, hydrogen bonds, and van der Waals forces are key drivers of LEV-protein binding.
  • LEV binding induced conformational changes in the secondary structures of LYZ, trypsin, and BHb, affecting their α-helix and β-sheet percentages.
  • Molecular docking revealed LEV binding to active sites of LYZ and trypsin, and the central cavity of BHb.
  • LEV decreased LYZ activity while increasing trypsin activity.

Conclusions:

  • Levofloxacin interacts with LYZ, trypsin, and BHb through a combination of forces, leading to structural modifications.
  • The binding sites and mechanisms vary among the studied proteins.
  • LEV binding influences the enzymatic activities of LYZ and trypsin, suggesting potential implications for their physiological roles.