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OJBTM

Online Journal of Bioinformatics ©

Volume 17(2):116-128, 2016.


 Molecular docking of indolizine heterocyclics

 

Murali Krishna K1, Lekha P2, Raman PK1, Raveendra Reddy P1.

 

1.Department of Chemistry, Sri Krishnadevaraya University, Ananthapuramu – 515 003. A.P., India

2. SVU college of engineering,sri venkateswara university,tirupati-517502.

                                                                                                                                                           

ABSTRACT

 

Murali Krishna K, Lekha P, Raman PK, Raveendra Reddy P., Molecular docking of indolizine heterocyclics, Onl J Bioinform., 17(2):116-128, 2016. Binding inhibitors using 3D structure of Staphylococcus aureus guanylate kinase as target are described. Inhibitor binding positions and affinities were determined using GOLD scoring fitness functions. We identified amino acid residues SER 112, PRO 113, THR 115, TYR 116, GLY 121 in Guanylate kinase that could affect inhibitor recognition via hydrogen bonding interactions. The docking results agreed with in vitro data, wherein anti-microbial activity of the analogues was higher than other drugs forming 5 hydrogen bonds. The docking study revealed the binding orientation of compounds in the Guanylate kinase of Staphylococcus aureus binding pocket surrounding the active site, which resulted in inhibition of enzyme activity.

 

Key words: Docking, insilico studies, Penicillin binding protein, Indolizine based heterocyclics.


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