ISSN

0974-4150 (Online)
0974-4169 (Print)


Author(s): Manojkumar R. Patle, S. H. Ganatra

Email(s): manojpatle14@gmail.com

DOI: Not Available

Address: Manojkumar R. Patle1* and S. H. Ganatra2
1Assistant Professor, Department of Chemistry, D. B. Science College, Gondia.
2Institute of Science. Nagpur
*Corresponding Author

Published In:   Volume - 4,      Issue - 6,     Year - 2011


ABSTRACT:
Tuberculosis (TB), a chronic bacterial infection, causes more deaths worldwide than any other infectious disease. TB is spread through the air and usually infects the lungs, although other organs are also involved in some cases. Some 2 billion people, nearly one-third of the world's population are infected with the TB organism, Mycobacterium tuberculosis. The Aim of the Research work is to detect potent anti-tuberculosis molecules by using the current technologies available in Computer Aided Drug Design and to successfully pertain with the most promising targets in Tuberculosis Chemotherapy. The In-Silico inhibitions studies were carried out between Quinolinic Acid Phosphoribosyl transferase (PDB code: 1QPQ) enzyme (QAPRTase), a key enzyme in the de novo biosynthesis of NAD, as a receptor and series of derivatives of Phenothiazine as a substrate (ligand). The numbers of derivatives of substituted Phenothiazine based molecules were designed using Molecular Mechanics techniques by substituting different groups or atoms at R1, R2 R3 and R4 positions. The designed molecules were interacted with selected enzyme using computer simulation techniques. The free energy (?G) per mole was calculated. Among the studied molecules, a few numbers of derivatives show negative free energy and hence can be studied as potent Quinolinic Acid Phosphoribosyltransferase inhibitors.


Cite this article:
Manojkumar R. Patle, S. H. Ganatra. In-Silico Inhibition Studies of Phenothiazine Based Compounds on Quinolinic Acid Phosphoribosyltransferase (1QPQ) Enzyme as A Potent Anti-Tuberculosis Agent. Asian J. Research Chem. 4(6): June, 2011; Page 990-996.


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