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Predicted binding of certain antifilarial compounds with glutathione-S-transferase of human Filariids

Glutathione-S-transferase is a major phase-II detoxification enzyme in parasitic helminthes. Previous research highlights the importance of GSTs in the establishment of chronic infections in cytotoxic microenvironments. Filarial nematodes depend on these detoxification enzymes for their survival in...

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Autores principales: Saeed, Mohd, Baig, Mohd Hassan, Bajpai, Preeti, Srivastava, Ashwini Kumar, Ahmad, Khurshid, Mustafa, Huma
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3602877/
https://www.ncbi.nlm.nih.gov/pubmed/23516334
http://dx.doi.org/10.6026/97320630009233
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author Saeed, Mohd
Baig, Mohd Hassan
Bajpai, Preeti
Srivastava, Ashwini Kumar
Ahmad, Khurshid
Mustafa, Huma
author_facet Saeed, Mohd
Baig, Mohd Hassan
Bajpai, Preeti
Srivastava, Ashwini Kumar
Ahmad, Khurshid
Mustafa, Huma
author_sort Saeed, Mohd
collection PubMed
description Glutathione-S-transferase is a major phase-II detoxification enzyme in parasitic helminthes. Previous research highlights the importance of GSTs in the establishment of chronic infections in cytotoxic microenvironments. Filarial nematodes depend on these detoxification enzymes for their survival in the host. GST plays an important role in filariasis and other diseases. GST from W.bancrofti and B.malayi are very much different from human GST. This structural difference makes GST potential chemotherapeutic targets for antifilarial treatment. In this study we have checked the efficacy of some well known antifilarial compounds against GST from B.malayi and W.bancrofti. The structure of BmGST was modeled using modeller9v10 and was submitted to PMDB. Molecular docking study reveals arbindazole to be the most potent compounds against GST from both the filarial parasites. Role of some residues playing important role in the binding of compounds within the active site of GST has also been revealed in the present study. The BmGST and WbGST structural information and docking studies could aid in screening new antifilarials or selective inhibitors for chemotherapy against filariasis. ABBREVIATIONS: GST - Glutathione-S-transferase, Bm - Brugia malayi, Wb - Wuchereria bancrofti.
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spelling pubmed-36028772013-03-20 Predicted binding of certain antifilarial compounds with glutathione-S-transferase of human Filariids Saeed, Mohd Baig, Mohd Hassan Bajpai, Preeti Srivastava, Ashwini Kumar Ahmad, Khurshid Mustafa, Huma Bioinformation Hypothesis Glutathione-S-transferase is a major phase-II detoxification enzyme in parasitic helminthes. Previous research highlights the importance of GSTs in the establishment of chronic infections in cytotoxic microenvironments. Filarial nematodes depend on these detoxification enzymes for their survival in the host. GST plays an important role in filariasis and other diseases. GST from W.bancrofti and B.malayi are very much different from human GST. This structural difference makes GST potential chemotherapeutic targets for antifilarial treatment. In this study we have checked the efficacy of some well known antifilarial compounds against GST from B.malayi and W.bancrofti. The structure of BmGST was modeled using modeller9v10 and was submitted to PMDB. Molecular docking study reveals arbindazole to be the most potent compounds against GST from both the filarial parasites. Role of some residues playing important role in the binding of compounds within the active site of GST has also been revealed in the present study. The BmGST and WbGST structural information and docking studies could aid in screening new antifilarials or selective inhibitors for chemotherapy against filariasis. ABBREVIATIONS: GST - Glutathione-S-transferase, Bm - Brugia malayi, Wb - Wuchereria bancrofti. Biomedical Informatics 2013-03-02 /pmc/articles/PMC3602877/ /pubmed/23516334 http://dx.doi.org/10.6026/97320630009233 Text en © 2013 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Saeed, Mohd
Baig, Mohd Hassan
Bajpai, Preeti
Srivastava, Ashwini Kumar
Ahmad, Khurshid
Mustafa, Huma
Predicted binding of certain antifilarial compounds with glutathione-S-transferase of human Filariids
title Predicted binding of certain antifilarial compounds with glutathione-S-transferase of human Filariids
title_full Predicted binding of certain antifilarial compounds with glutathione-S-transferase of human Filariids
title_fullStr Predicted binding of certain antifilarial compounds with glutathione-S-transferase of human Filariids
title_full_unstemmed Predicted binding of certain antifilarial compounds with glutathione-S-transferase of human Filariids
title_short Predicted binding of certain antifilarial compounds with glutathione-S-transferase of human Filariids
title_sort predicted binding of certain antifilarial compounds with glutathione-s-transferase of human filariids
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3602877/
https://www.ncbi.nlm.nih.gov/pubmed/23516334
http://dx.doi.org/10.6026/97320630009233
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