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OJBTM
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.
ABSTRACT
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.
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