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Online Journal of Bioinformatics ©
Volume 16 (1): 88-97, 2015.
In silico docking of meliantrol, β-sitosterol, curcumin, vanillic and syringic acids to
penicillin binding protein 2a on methicillin resistant Staphylococcus aureus.
Hajera Masroor1., M.Parvateesam2., Jayasimha Rayalu Daddam3*., N.V.Naidu4
1, 2, 4 Global Institute of Biotechnology, Sai Triveni Chambers, 3Department of Biotechnology, Akshaya Biological Corporation, Himayath nagar, Hyderabd, India.
Masroor H, Parvateesam M, Daddam JR, Naidu NV., In silico docking of meliantrol, β-sitosterol, curcumin, vanillic and syringic acids to penicillin binding protein 2a on methicillin resistant Staphylococcus aureus, Onl J Bioinform., 16 (1): 88-97, 2015. We report In silico binding of Meliantrol, β-sitosterol, Circumin, Vanillic and Syringic acids on Pencillin Binding Protein 2a (PBP2a) of Methicillin Resistant Staphylococcus aureus. The crystal structure of PBP2a was taken from Protein Data Bank (PDB_ID:1VQQ) and potential binding sites of PBP2a were searched with CASTP server. Molecular docking was then performed using Genetic Optimization of Ligand Docking software to determine the binding orientation of compounds into PBP2a structure. The efficiency and drug-likeness of various plant compounds were identified using pre-ADMET software. Results suggested that all docked compounds were found to have some interaction between an oxygen atom of the Compounds and PBP2a. In the binding pocket, common H-bonding interactions were formed between all docked compounds and GLY 135, GLN 137, GLN 140, HIS 143, GLU 145, GLN 145, GLN 207, ASP 209, HIS 232, THR 300, and HIS 311. Docking results agreed with observed In vitro data, revealing that the PBP2a inhibitory activity of Curcumin was higher than other tested compounds.
Keywords: MRSA, PBP2a, Docking, Curcumin and ADMET studies.