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OJBTM
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.
ABSTRACT
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:
3.3.1.1) (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.
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