MAIN


1996-2019. All Rights Reserved. Online Journal of Bioinformatics . You may not store these pages in any form except for your own personal use. All other usage or distribution is illegal under international copyright treaties. Permission to use any of these pages in any other way besides the  before mentioned must be gained in writing from the publisher. This article is exclusively copyrighted in its entirety to OJB publications. This article may be copied once but may not be, reproduced or  re-transmitted without the express permission of the editors. This journal satisfies the refereeing requirements (DEST) for the Higher Education Research Data Collection (Australia). Linking: To link to this page or any pages linking to this page you must link directly to this page only here rather than put up your own page.


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.


MAIN

 

FULL-TEXT(SUBSCRIPTION OR PURCHASE TITLE $25USD)