Investigating the molecular mechanism of staphylococcal DNA gyrase inhibitors: A combined ligand-based and structure-based resources pipeline

J Mol Graph Model. 2018 Oct:85:122-129. doi: 10.1016/j.jmgm.2018.07.010. Epub 2018 Jul 27.

Abstract

Appropriate therapeutic solutions against Staphylococcal infections are currently limited. To work out the complex task of challenging drug resistance in Staphylococcus aureus, new compounds with novel modes of action are required. In this study, we performed target-driven virtual screening to filter exhaustive phytochemical libraries that can inhibit the activity of S. aureus DNA Gyrase B (Gyr B). Three top-ranked hit molecules (Mangostenone E, Candenatenin A and 2,4,4'-trihydroxydihydrochalcone) were identified from comprehensive molecular docking studies based on their strong spatial affinity with key catalytic residues of the binding pocket of DNA GyrB, especially with the well-known crucial residue Asp81. Molecular dynamics (MD) simulations were performed for these identified hit molecules for better understanding of their dynamical and structural profiles throughout the MD simulations. These compounds can be explored as future lead optimization molecules to discover a new class of antibiotics against resistant Staphylococcus aureus strains.

Keywords: Candenatenin A; DNA gyrase subunit B; Drug resistance; Mangostenone E; Molecular docking; Molecular dynamic (MD) simulations; Phytochemicals; Staphylococcus aureus.

MeSH terms

  • Antineoplastic Agents / chemistry*
  • Antineoplastic Agents / pharmacology
  • Binding Sites
  • DNA Gyrase / chemistry*
  • Drug Resistance, Bacterial
  • Ligands
  • Molecular Docking Simulation*
  • Molecular Dynamics Simulation*
  • Protein Binding
  • Quantitative Structure-Activity Relationship
  • Staphylococcus aureus / drug effects
  • Staphylococcus aureus / enzymology*

Substances

  • Antineoplastic Agents
  • Ligands
  • DNA Gyrase