Leishmanicidal Activity of an In Silico -Screened Novel Inhibitor against Ascorbate Peroxidase of Leishmania donovani-Reference-Cited by-同舟云学术

Leishmanicidal Activity of an In Silico -Screened Novel Inhibitor against Ascorbate Peroxidase of Leishmania donovani

Published:2020-06-23 Issue:7 Volume:64 Page:
ISSN:0066-4804
Container-title:Antimicrobial Agents and Chemotherapy
language:en
Short-container-title:Antimicrob Agents Chemother

Author:

Kashif Mohammad¹,Paladhi Ankush²,Singh Ranjeet¹,Bhattacharyya Sankar³,Hira Sumit Kumar²^ORCID,Manna Partha Pratim¹^ORCID

Affiliation:

1. Immunobiology Laboratory, Department of Zoology, Institute of Science, Banaras Hindu University, Varanasi, India

2. Cellular Immunology Laboratory, Department of Zoology, The University of Burdwan, Purba Bardhhaman, India

3. Immunobiology Lab, Department of Zoology, Sidho Kanho Birsha University, Purulia, India

Abstract

Peroxidases are a heterogeneous family of enzymes that have diverse biological functions. Ascorbate peroxidase is a redox enzyme that is reduced by trypanothione, which plays a central role in the redox defense system of Leishmania . In view of developing new and novel therapeutics, we performed in silico studies in order to search for a ligand library and identify new drug candidates and their physiological roles against promastigotes and intracellular amastigotes of Leishmania donovani .

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Link

https://journals.asm.org/doi/pdf/10.1128/AAC.01766-19

Reference38 articles.

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2. Overexpression of Mitochondrial Leishmania major Ascorbate Peroxidase Enhances Tolerance to Oxidative Stress-Induced Programmed Cell Death and Protein Damage

3. Ascorbate Peroxidase from Leishmania major Controls the Virulence of Infective Stage of Promastigotes by Regulating Oxidative Stress

4. Proteome changes associated with Leishmania donovani promastigote adaptation to oxidative and nitrosative stresses

5. Specific Inhibition of p97/VCP ATPase and Kinetic Analysis Demonstrate Interaction between D1 and D2 ATPase Domains

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