IDENTIFICATION OF NOVEL INHIBITORS AGAINST POTENTIAL TARGETS OF CAMPYLOBACTER JEJUNI

  • Anukriti Verma Amity Institute of Biotechnology J-3 Block, Amity University Campus, Sector–125, Noida 201303 (U. P.)
  • Bhawna Rathi Amity Institute of Biotechnology J-3 Block, Amity University Campus, Sector–125, Noida 201303 (U. P.)
  • Shivani Sharda Amity Institute of Biotechnology J-3 Block, Amity University Campus, Sector–125, Noida 201303 (U. P.)

Abstract

Objective: The aim of the present study is the structure identification of UDP-N-acetyl muramate dehydrogenase and 4-hydroxy-3-methylbut-2-enyl diphosphate reductase for Campylobacter jejuni and designing their inhibitors using docking and simulation studies.

Methods: Uniprot, BLAST P, Discovery Studio, Verify 3D and Maestro Schrödinger suit have been used for structure identification, validation and docking studies.

Results: The structures of UDP-N-acetylmuramic dehydrogenase and 4-hydroxy-3-methylbut-2-enyl diphosphate reductase were predicted and validated generating 87.80% and 85.82% score respectively. For 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, HTVS resulted in 5801 compounds while SP and XP resulted in 5781 ligands. For UDP-N-acetylmuramate dehydrogenase, HTVS resulted in 5474 compounds whereas SP and XP resulted in 5359 ligands.

Conclusion: The structures of UDP-N-acetylmuramate dehydrogenase and 4-hydroxy-3-methylbut-2-enyl diphosphate reductase were detected and verified. The list of top 10 inhibitors was acquired that can be considered as putative and potential drug targets.

Keywords: Campylobacter jejuni, Structure prediction, Active site, Docking, Inhibitor.

 

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How to Cite
Verma, A., B. Rathi, and S. Sharda. “IDENTIFICATION OF NOVEL INHIBITORS AGAINST POTENTIAL TARGETS OF CAMPYLOBACTER JEJUNI”. International Journal of Pharmacy and Pharmaceutical Sciences, Vol. 8, no. 2, Feb. 2016, pp. 312-6, https://innovareacademics.in/journals/index.php/ijpps/article/view/9284.
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