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Biochemical efficacy, molecular docking and inhibitory effect of 2, 3-dimethylmaleic anhydride on insect acetylcholinesterase

Evolution of resistance among insects to action of pesticides has led to the discovery of several insecticides (neonicotinoids and organophosphates) with new targets in insect nervous system. Present study evaluates the mode of inhibition of acetylchlonesterase (AChE), biochemical efficacy, and mole...

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Autores principales: Singh, Kabrambam D., Labala, Rajendra K., Devi, Thiyam B., Singh, Ningthoujam I., Chanu, Heisnam D., Sougrakpam, Sonia, Nameirakpam, Bunindro S., Sahoo, Dinabandhu, Rajashekar, Yallappa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5624869/
https://www.ncbi.nlm.nih.gov/pubmed/28970561
http://dx.doi.org/10.1038/s41598-017-12932-0
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author Singh, Kabrambam D.
Labala, Rajendra K.
Devi, Thiyam B.
Singh, Ningthoujam I.
Chanu, Heisnam D.
Sougrakpam, Sonia
Nameirakpam, Bunindro S.
Sahoo, Dinabandhu
Rajashekar, Yallappa
author_facet Singh, Kabrambam D.
Labala, Rajendra K.
Devi, Thiyam B.
Singh, Ningthoujam I.
Chanu, Heisnam D.
Sougrakpam, Sonia
Nameirakpam, Bunindro S.
Sahoo, Dinabandhu
Rajashekar, Yallappa
author_sort Singh, Kabrambam D.
collection PubMed
description Evolution of resistance among insects to action of pesticides has led to the discovery of several insecticides (neonicotinoids and organophosphates) with new targets in insect nervous system. Present study evaluates the mode of inhibition of acetylchlonesterase (AChE), biochemical efficacy, and molecular docking of 2,3-dimethylmaleic anhydride, against Periplaneta americana and Sitophilus oryzae. The knockdown activity of 2,3-dimethylmaleic anhydride was associated with in vivo inhibition of AChE. At KD(99) dosage, the 2,3-dimethylmaleic anhydride showed more than 90% inhibition of AChE activity in test insects. A significant impairment in antioxidant system was observed, characterized by alteration in superoxide dismutase and catalase activities along with increase in reduced glutathione levels. Computational docking programs provided insights in to the possible interaction between 2,3-dimethylmaleic anhydride and AChE of P. americana. Our study reveals that 2,3-dimethylmaeic anhydride elicits toxicity in S. oryzae and P. americana primarily by AChE inhibition along with oxidative stress.
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spelling pubmed-56248692017-10-12 Biochemical efficacy, molecular docking and inhibitory effect of 2, 3-dimethylmaleic anhydride on insect acetylcholinesterase Singh, Kabrambam D. Labala, Rajendra K. Devi, Thiyam B. Singh, Ningthoujam I. Chanu, Heisnam D. Sougrakpam, Sonia Nameirakpam, Bunindro S. Sahoo, Dinabandhu Rajashekar, Yallappa Sci Rep Article Evolution of resistance among insects to action of pesticides has led to the discovery of several insecticides (neonicotinoids and organophosphates) with new targets in insect nervous system. Present study evaluates the mode of inhibition of acetylchlonesterase (AChE), biochemical efficacy, and molecular docking of 2,3-dimethylmaleic anhydride, against Periplaneta americana and Sitophilus oryzae. The knockdown activity of 2,3-dimethylmaleic anhydride was associated with in vivo inhibition of AChE. At KD(99) dosage, the 2,3-dimethylmaleic anhydride showed more than 90% inhibition of AChE activity in test insects. A significant impairment in antioxidant system was observed, characterized by alteration in superoxide dismutase and catalase activities along with increase in reduced glutathione levels. Computational docking programs provided insights in to the possible interaction between 2,3-dimethylmaleic anhydride and AChE of P. americana. Our study reveals that 2,3-dimethylmaeic anhydride elicits toxicity in S. oryzae and P. americana primarily by AChE inhibition along with oxidative stress. Nature Publishing Group UK 2017-10-02 /pmc/articles/PMC5624869/ /pubmed/28970561 http://dx.doi.org/10.1038/s41598-017-12932-0 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Singh, Kabrambam D.
Labala, Rajendra K.
Devi, Thiyam B.
Singh, Ningthoujam I.
Chanu, Heisnam D.
Sougrakpam, Sonia
Nameirakpam, Bunindro S.
Sahoo, Dinabandhu
Rajashekar, Yallappa
Biochemical efficacy, molecular docking and inhibitory effect of 2, 3-dimethylmaleic anhydride on insect acetylcholinesterase
title Biochemical efficacy, molecular docking and inhibitory effect of 2, 3-dimethylmaleic anhydride on insect acetylcholinesterase
title_full Biochemical efficacy, molecular docking and inhibitory effect of 2, 3-dimethylmaleic anhydride on insect acetylcholinesterase
title_fullStr Biochemical efficacy, molecular docking and inhibitory effect of 2, 3-dimethylmaleic anhydride on insect acetylcholinesterase
title_full_unstemmed Biochemical efficacy, molecular docking and inhibitory effect of 2, 3-dimethylmaleic anhydride on insect acetylcholinesterase
title_short Biochemical efficacy, molecular docking and inhibitory effect of 2, 3-dimethylmaleic anhydride on insect acetylcholinesterase
title_sort biochemical efficacy, molecular docking and inhibitory effect of 2, 3-dimethylmaleic anhydride on insect acetylcholinesterase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5624869/
https://www.ncbi.nlm.nih.gov/pubmed/28970561
http://dx.doi.org/10.1038/s41598-017-12932-0
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