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Online Journal of Bioinformatics ©
Volume 17(2):148-158, 2016..
In silico binding and inhibition of Sortase A of methicillin resistant Staphylococcus aureus.
Suhas Souri J1, Ashish Kumar Sharma2, Gaurav Sharma3
1,2Department(s) of Pharmacology, NIMS Institute of Pharmacy, 3Microbiology, Suresh Gyan Vihar University, Shobha Nagar, Jaipur, Rajasthan, India.
Souri S, Sharma AK, Sharma G., In silico binding and inhibition of Sortase A methicillin resistant Staphylococcus aureus, Onl J Bioinform., 17(2):148-158, 2016. Plant derived conjugated linoleic (18:2) acid, thymoquinone, nigellone (dithymoquinone), melanthin, nigilline, damascenine and tannins were assessed for In silico binding and inhibition of Sortase A of methicillin resistant Staphylococcus aureus by computational methods. Crystal structure of Sortase A was derived from Protein Data Bank (PDB_ID:1T2W) and potential binding sites were searched with CASTP server. Molecular docking was done by genetic optimization of ligand docking based algorithm to determine binding orientation of compounds to Sortase A. The efficiency and drug-likeness of the compounds were identified using pre-ADMET software. The oxygen atom of all compounds interacted with Sortase A structure. In the binding pocket, common H-bonding interactions formed between all docked compounds and ASP-65, CYS-66, CYS-88. Docking results confirmed observed In vitro data showing that Sortase A inhibitory activity of dithymoquinone was highest compared with other compounds tested.
Keywords: MRSA, Sortase A, Docking, dithymoquinone and ADMET studies.