- Title
- Molecular docking interaction of mycobacterium tuberculosis lipb enzyme with isoniazid, pyrazinamide and a structurally altered drug 2, 6 dimethoxyisonicotinohydrazide
- Creator
- Namasivayam, Muthuraman
- Date
- 2015
- Type
- Text; Journal article
- Identifier
- http://researchonline.federation.edu.au/vital/access/HandleResolver/1959.17/181757
- Identifier
- vital:16021
- Identifier
-
https://doi.org/10.11648/j.cbb.20150304.11
- Identifier
- ISBN:2330-8265
- Abstract
- Tuberculosis is an infectious airborne disease caused by a bacterial infection that affects the lungs and other parts of the body. Vaccination against tuberculosis is available but proved to be unsuccessful against emerging multi drug and extensive drug resistant bacterial strains. This in turn raises the pressure to speed up the research on developing new and more efficient anti-tuberculosis drugs. Lipoate biosynthesis protein B (LipB) is found to play vital role in the lipoylation process in Mycobacterium tuberculosis and thus making it a very promising drug target. The existing first line drugs such as Isoniazid, Pyrazinamide and Rifampicin etc shows only profound binding affinity with this target protein. Therefore, new or modified drugs with better docking approach that exhibit a closer and stronger binding affinity is essential. This current study opens up a novel approach towards anti-tuberculosis agents by determining drugs that share similar structures with some of the best available first line drug and also happen to possess better binding affinity. In this article, a computational method by which, pristine as well certain first line and structurally modified drugs were docked with the LipB protein target; where, structurally modified 2, 6 Dimethoxyisonicotinohydrazide show superior target docking.
- Relation
- Computational biology and bioinformatics (Print) Vol. 3, no. 4 (2015), p. 45
- Rights
- All metadata describing materials held in, or linked to, the repository is freely available under a CC0 licence
- Rights
- http://creativecommons.org/licenses/by/4.0/
- Rights
- Copyright @ Science Publishing Group
- Rights
- Open Access
- Subject
- 31 Biological Sciences; 46 Information and Computing Sciences; 49 Mathematical Sciences
- Full Text
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