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Online Journal of Bioinformatics ©
Volume 17(1):41-52, 2016
Homology modelling and structure for Neplanocin A derivatives
Dilibe Clifford Urama1, Sanjeeva Prasad Tarigopula2, K. Mehraj Pasha3, Jayasimha Rayalu Daddam4*
1Department(s) of genetics and Biotechnology, Osmania University, Hyderabad, 2Zoology, Sri Krishnadevaraya University, Anantapur, Andhra Pradesh, Humanities & Science, Kuppam Engineering College, Kuppam, 4Bioinformatics, Global Institute of Biotechnology, Himayath nagar, Hyd-29, India.
Urama DC, Tarigopula SP, Pasha KM, Daddam JR., Homology modelling and structure of Neplanocin A derivative., Onl J Bioinform., 17(1):41-52, 2016. Neplanocin A cyclopentenyl analog of adenosine is a naturally occurring antibiotic with antitumor activity. We demonstrate why neplanocin A derivatives could inhibitit S-adenosylhomocysteine (AdoHcy) hydrolase. Neplanocin A may inhibit vaccinia virus by affecting S-adenosylmethionine-dependent macromolecular methylation required for production of new virus particles by viral messenger RNA. Adverse effects were reduced by docking substitutes of Neoplacin with GOLD software. Irreversible inactivation of AdoHcy hydrolase by neplanocin A suggested tight binding stoichiometry of 1 to 1 molecule (tetramer) with enzyme. Binding of Neoplacin A with S-adenosyl-L-homocysteine hydrolase (EC: 126.96.36.199) (AdoHcyase) substituted with 5’-fluoro-Neplanocin generated a high binding energy of 38.23 kcal/mol. Pharmacophore mapping and ludi interaction for strengthening the binding of ligand with S-adenosyl-L-homocysteine hydrolase generated 5’-fluoro-Neplanocin A with best fit score.
Key words: Neplanocin A, Modelling, S-adenosylhomocysteine, Docking studies.