Theoretical evaluation of the malathion and its chemical derivatives interaction with cytosolic phospholipase A2 from zebrafish
Autor(a) principal: | |
---|---|
Data de Publicação: | 2023 |
Outros Autores: | , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.chemosphere.2022.136984 http://hdl.handle.net/11449/247814 |
Resumo: | Cytosolic phospholipase A2 (cPLA2) belongs to a large family of proteins and plays a crucial role in the regulation of arachidonic acid metabolism and inflammation cascade in zebrafish (Danio rerio). This enzyme with a molecular weight of 85 kDa, has two distinct domains. One is the regulatory and calcium-dependent (Ca2+) domain called C2, the other is the catalytic α/β hydrolase Ca2+-independent domain, where serine and aspartic acid catalytic dyad residues are present. We investigated the interaction of malathion and their organophosphate metabolites in the cPLA2 using in silico tools. Molecular docking results showed hydrophobic interactions with the paraoxon and catalytic site residue (Ser 223). Malathion increases intracellular Ca2+ due to endoplasmic reticulum influx which in turn activities phospholipase A2 and arachidonic acid release. Molecular docking and homology modelling of proteins and ligands could be a complementary tool for ecotoxicology and environment pollution assessment. |
id |
UNSP_0213cee3ac708c8c909e53096b6d5376 |
---|---|
oai_identifier_str |
oai:repositorio.unesp.br:11449/247814 |
network_acronym_str |
UNSP |
network_name_str |
Repositório Institucional da UNESP |
repository_id_str |
2946 |
spelling |
Theoretical evaluation of the malathion and its chemical derivatives interaction with cytosolic phospholipase A2 from zebrafishDocking molecularOrganophosphatesPhospholipase A2XenobioticsCytosolic phospholipase A2 (cPLA2) belongs to a large family of proteins and plays a crucial role in the regulation of arachidonic acid metabolism and inflammation cascade in zebrafish (Danio rerio). This enzyme with a molecular weight of 85 kDa, has two distinct domains. One is the regulatory and calcium-dependent (Ca2+) domain called C2, the other is the catalytic α/β hydrolase Ca2+-independent domain, where serine and aspartic acid catalytic dyad residues are present. We investigated the interaction of malathion and their organophosphate metabolites in the cPLA2 using in silico tools. Molecular docking results showed hydrophobic interactions with the paraoxon and catalytic site residue (Ser 223). Malathion increases intracellular Ca2+ due to endoplasmic reticulum influx which in turn activities phospholipase A2 and arachidonic acid release. Molecular docking and homology modelling of proteins and ligands could be a complementary tool for ecotoxicology and environment pollution assessment.Instituto de Biociências Universidade Estadual Paulista (UNESP), São VicenteBIOMOLPEP Instituto de Biociências Universidade Estadual Paulista (UNESP), São VicenteUniversidade Paulista UNIP SantosDepartamento de Articulação Estratégica de Vigilância em Saúde (DAEVS)Instituto de Biociências Universidade Estadual Paulista (UNESP), São VicenteBIOMOLPEP Instituto de Biociências Universidade Estadual Paulista (UNESP), São VicenteUniversidade Estadual Paulista (UNESP)SantosManzi, Agatha [UNESP]De-Carli, Bruno Paes [UNESP]Roggero, Airam [UNESP]Ferreira De Moraes, Laila Lucyane [UNESP]Annunciato, Isabelly [UNESP]Novo Belchor, Mariana [UNESP]Lima Neto, Daniel Ferreira DeAntonio De Oliveira, Marcos [UNESP]Hikari Toyama, Marcos [UNESP]2023-07-29T13:26:38Z2023-07-29T13:26:38Z2023-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.chemosphere.2022.136984Chemosphere, v. 311.1879-12980045-6535http://hdl.handle.net/11449/24781410.1016/j.chemosphere.2022.1369842-s2.0-85140894081Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengChemosphereinfo:eu-repo/semantics/openAccess2023-07-29T13:26:38Zoai:repositorio.unesp.br:11449/247814Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-07-29T13:26:38Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Theoretical evaluation of the malathion and its chemical derivatives interaction with cytosolic phospholipase A2 from zebrafish |
title |
Theoretical evaluation of the malathion and its chemical derivatives interaction with cytosolic phospholipase A2 from zebrafish |
spellingShingle |
Theoretical evaluation of the malathion and its chemical derivatives interaction with cytosolic phospholipase A2 from zebrafish Manzi, Agatha [UNESP] Docking molecular Organophosphates Phospholipase A2 Xenobiotics |
title_short |
Theoretical evaluation of the malathion and its chemical derivatives interaction with cytosolic phospholipase A2 from zebrafish |
title_full |
Theoretical evaluation of the malathion and its chemical derivatives interaction with cytosolic phospholipase A2 from zebrafish |
title_fullStr |
Theoretical evaluation of the malathion and its chemical derivatives interaction with cytosolic phospholipase A2 from zebrafish |
title_full_unstemmed |
Theoretical evaluation of the malathion and its chemical derivatives interaction with cytosolic phospholipase A2 from zebrafish |
title_sort |
Theoretical evaluation of the malathion and its chemical derivatives interaction with cytosolic phospholipase A2 from zebrafish |
author |
Manzi, Agatha [UNESP] |
author_facet |
Manzi, Agatha [UNESP] De-Carli, Bruno Paes [UNESP] Roggero, Airam [UNESP] Ferreira De Moraes, Laila Lucyane [UNESP] Annunciato, Isabelly [UNESP] Novo Belchor, Mariana [UNESP] Lima Neto, Daniel Ferreira De Antonio De Oliveira, Marcos [UNESP] Hikari Toyama, Marcos [UNESP] |
author_role |
author |
author2 |
De-Carli, Bruno Paes [UNESP] Roggero, Airam [UNESP] Ferreira De Moraes, Laila Lucyane [UNESP] Annunciato, Isabelly [UNESP] Novo Belchor, Mariana [UNESP] Lima Neto, Daniel Ferreira De Antonio De Oliveira, Marcos [UNESP] Hikari Toyama, Marcos [UNESP] |
author2_role |
author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (UNESP) Santos |
dc.contributor.author.fl_str_mv |
Manzi, Agatha [UNESP] De-Carli, Bruno Paes [UNESP] Roggero, Airam [UNESP] Ferreira De Moraes, Laila Lucyane [UNESP] Annunciato, Isabelly [UNESP] Novo Belchor, Mariana [UNESP] Lima Neto, Daniel Ferreira De Antonio De Oliveira, Marcos [UNESP] Hikari Toyama, Marcos [UNESP] |
dc.subject.por.fl_str_mv |
Docking molecular Organophosphates Phospholipase A2 Xenobiotics |
topic |
Docking molecular Organophosphates Phospholipase A2 Xenobiotics |
description |
Cytosolic phospholipase A2 (cPLA2) belongs to a large family of proteins and plays a crucial role in the regulation of arachidonic acid metabolism and inflammation cascade in zebrafish (Danio rerio). This enzyme with a molecular weight of 85 kDa, has two distinct domains. One is the regulatory and calcium-dependent (Ca2+) domain called C2, the other is the catalytic α/β hydrolase Ca2+-independent domain, where serine and aspartic acid catalytic dyad residues are present. We investigated the interaction of malathion and their organophosphate metabolites in the cPLA2 using in silico tools. Molecular docking results showed hydrophobic interactions with the paraoxon and catalytic site residue (Ser 223). Malathion increases intracellular Ca2+ due to endoplasmic reticulum influx which in turn activities phospholipase A2 and arachidonic acid release. Molecular docking and homology modelling of proteins and ligands could be a complementary tool for ecotoxicology and environment pollution assessment. |
publishDate |
2023 |
dc.date.none.fl_str_mv |
2023-07-29T13:26:38Z 2023-07-29T13:26:38Z 2023-01-01 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.chemosphere.2022.136984 Chemosphere, v. 311. 1879-1298 0045-6535 http://hdl.handle.net/11449/247814 10.1016/j.chemosphere.2022.136984 2-s2.0-85140894081 |
url |
http://dx.doi.org/10.1016/j.chemosphere.2022.136984 http://hdl.handle.net/11449/247814 |
identifier_str_mv |
Chemosphere, v. 311. 1879-1298 0045-6535 10.1016/j.chemosphere.2022.136984 2-s2.0-85140894081 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Chemosphere |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1803649369139838976 |