alexa In Silico Study of the Selective Inhibition of Bacterial Peptide Deformylases by Several Drugs
ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
Open Access

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Research Article

In Silico Study of the Selective Inhibition of Bacterial Peptide Deformylases by Several Drugs

Abdelouahab Chikhi* and Abderrahmane Bensegueni

Department of biochemistry-microbiology Faculty of natural andlife sciences, Mentouri University, Constantine, Algeria

*Corresponding Author:
Dr. Abdelouahab Chikhi
Department of biochemistry- microbiology Faculty of natural and life sciences
Mentouri University, Constantine, Algeria
Tel: + 213-793-112-547
E-mail: [email protected], [email protected]

Received Date: December 29, 2009; Accepted Date: February 13, 2010; Published Date: February 15, 2010

Citation: Chikhi A, Bensegueni A (2010) In Silico Study of the Selective Inhibition of Bacterial Peptide Deformylases by Several Drugs. J Proteomics Bioinform 3: 061-065. doi: 10.4172/jpb.1000122

Copyright: © 2010 Chikhi A, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

Abstract

To counter increasing levels of pathogen resistance new classes of antibiotics are needed without delay. The metalloenzyme peptide deformylase (PDF) correspond to one of the most promising bacterial targets in the search for novel mode of antibiotics action and was firstly selected as a specific bacterial target. Peptide analogs were developed as inhibitors containing a hydroxamate or formyl- hydroxylamine as metal interacting group, and used as inhibitors with in vitro activity against a broad spectrum of organisms and successful antibacterial activity in vivo that is harmonizing with good pharmacokinetic properties and excellent tolerability in diverse species, but a human homologue was recently discovered. A new strategy for selecting highly efficient compounds with low inhibition effect against human PDF was developed. An original class of small, non-peptidic inhibitors of peptide deformylase (PDF) as potent antibiotics such as indol-group and its derivatives with the same mode of action in vivo as previously identified PDF inhibitors but without the apoptotic effects of these inhibitors in human cells, has been discovered. This study has confirmed the selective action of these compounds on bacterial PDFs by docking method using the autodock program. Indeed, a good correlation between IC50 and deltaG values of different complexes PDF-inhibitors was observed. The evaluation of the various molecular properties of these inhibitors lets us conclude that all these compounds are most likely drugable.

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