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Identification of New Enterococcus faecalis Peptide Deformylase Inhibitors

[ Vol. 15 , Issue. 2 ]

Author(s):

Amina Merzoug*, Abdelouahab Chikhi, Abderrahmane Bensegueni, Hanane Boucherit and Sawsen Hadef   Pages 120 - 132 ( 13 )

Abstract:


Aim and Objective: The antibacterial therapy resistance poses an urgent threat to the public’s health. Peptide deformylase is a favorable target to identify new antibiotics with novel mechanism of action.

Materials and Methods: In order to discovery new potent inhibitors of this enzyme, the virtual screening method of Zinc database using the binding site of Enterococcus faecalis peptide deformylase combined with microbiological assay were realized.

Results: The strategy undertaken in this study allowed us to identify new products with growth inhibition activity. The best result was obtained for the chemicals 4-(1,3-dioxo-1Hbenzo[de]isoquinolin- 2(3H)-yl)-N-hydroxybutanamide and N-hydroxy-2-(3-oxo-3,4-dihydro-2H-1,4-benzothiazin-2-yl) acetamide, they showed good affinities and great antibacterial activities compared to the other studied products.

Conclusion: The two most promising compounds can serve as potential antibacterial agents.

Keywords:

Antibacterial activity, binding affinity, Enterococcus faecalis, peptide deformylase, virtual screening, ZINC database.

Affiliation:

Laboratory of Applied Biochemistry, Department of Biochemistry and Cellular and Molecular Biology, Faculty of Natural and Life Sciences, Mentouri Brothers University, Constantine 1, Laboratory of Applied Biochemistry, Department of Biochemistry and Cellular and Molecular Biology, Faculty of Natural and Life Sciences, Mentouri Brothers University, Constantine 1 , Laboratory of Applied Biochemistry, Department of Biochemistry and Cellular and Molecular Biology, Faculty of Natural and Life Sciences, Mentouri Brothers University, Constantine 1 , Laboratory of Applied Biochemistry, Department of Biochemistry and Cellular and Molecular Biology, Faculty of Natural and Life Sciences, Mentouri Brothers University, Constantine 1, A. Boussouf University Center, Mila

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