Integrated Multi-omics, Virtual Screening and Molecular Docking Analysis of Methicillin-Resistant < em > Staphylococcus aureus < /em > USA300 for the Identification of Potential Therapeutic Targets: An In-Silico Approach

In this study, staphylococcal FemA protein (P0A0A5) is subjected to structure-based virtual screening for the drug repurposing approach. There are 20 residues missing in the crystal structure of FemA, and 12 of these residues are located at the catalytic site. The missing residues are modelled, and stereochemistry is checked. FDA approved drugs available in the DrugBank database have been used in virtual screening with FemA in search of potential repurposed molecules. This approach provides us with 10 drugs that may be used in the treatment of methicillin-resistant staphylococcal mediated diseases. AutoDock 4.2 is used for in silico screening and shows a comparable inhibition constant (Ki) for all 10 FDA-approved drugs towards FemA. Most of these drugs are used in the treatment of various cancers, migraines and leukaemia. Protein-drug interaction analysis shows that the drugs mostly interact with hydrophobic residues of FemA. Moreover, Tyr328 and Lys383 contribute largely to hydrogen bondings during interactions. All interacting amino acids that bind to the drugs are part of the active site cavity of FemA.SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10989-021-10287-9.PMID:34548853 | PMC:PMC8446483 | DOI:10.1007/s10989-021-10287-9
Source: Cell Research - Category: Cytology Authors: Source Type: research