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OJBTM
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.
ABSTRACT
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.
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