Mechanistics insights of hydrogen peroxide transport through PIP aquaporins pore

Autores
Chevriau, Jonathan; Zerbetto de Palma, Gerardo Gabriel; Zeida, Ari; Alleva, Karina Edith
Año de publicación
2021
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Hydrogen peroxide (H2O2) is transported through membranes by aquaporins (AQP). In particular, some plant PIP aquaporins isoforms are efficient H2O2 channels. As water and H2O2 share physicochemical features, it was first supposed that all AQP that transport water could act as an H2O2 channel. However, experimental evidence showed that not all PIP that transport water can transport H2O2. So, the mechanism of H2O2 transport is still an unsolved issue for AQP channels. MtPIP2,3 is a plasma membrane AQP from the legume Medicago truncatula that permeates H2O2. To understand the structural and chemical selectivity mechanisms leading to H2O2 permeability in PIPs, we characterized the particularities of H2O2 passingthrough MtPIP2,3 pore by 1 μs atomistic molecular dynamic simulations. As PIPs are tetrameric pH gated channels we constructed homology MtPIP2,3 models in open and closed states, and with or without H2O2. All models were conformationally stable along the simulation and H2O2 permeation events were found in the simulations in the presence of this molecule. We find that: i- H2O2 molecules can cross the pore in a single file, iidihedral angles adopted by H2O2 along the pore Z axis present a different distribution compared to the angles visited in the solution; in the selectivity-determining NPA region, H2O2 adopts the wider range of dihedral angles, iii- higher residence times are located around the selectivity filter zone in the open channel and moves to the cytoplasmic filterarea in the closed channel; and iv- the constriction in the cytoplasmic filter area seems to be more stringent for H2O2 passage than for water.Our results shed light onto the molecular mechanism of H2O2 passage through MtPIP2,3 and represent the first steps to understand the structural determinants of AQP differential selectivity for these molecules and water.
Fil: Chevriau, Jonathan. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Zerbetto de Palma, Gerardo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Zeida, Ari. Universidad de la República; Uruguay
Fil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
XLIX Reunión Anual de la Sociedad Argentina de Biofísica
Argentina
Sociedad Argentina de Biofisica
Materia
ACUAPORINAS
PEROXIDO DE HIDROGENO
TRANSPORTE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/196878
Acceder
id CONICETDig_dddf994743a65ef35288446b18193f5e
oai_identifier_str oai:ri.conicet.gov.ar:11336/196878
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Mechanistics insights of hydrogen peroxide transport through PIP aquaporins poreChevriau, JonathanZerbetto de Palma, Gerardo GabrielZeida, AriAlleva, Karina EdithACUAPORINASPEROXIDO DE HIDROGENOTRANSPORTEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Hydrogen peroxide (H2O2) is transported through membranes by aquaporins (AQP). In particular, some plant PIP aquaporins isoforms are efficient H2O2 channels. As water and H2O2 share physicochemical features, it was first supposed that all AQP that transport water could act as an H2O2 channel. However, experimental evidence showed that not all PIP that transport water can transport H2O2. So, the mechanism of H2O2 transport is still an unsolved issue for AQP channels. MtPIP2,3 is a plasma membrane AQP from the legume Medicago truncatula that permeates H2O2. To understand the structural and chemical selectivity mechanisms leading to H2O2 permeability in PIPs, we characterized the particularities of H2O2 passingthrough MtPIP2,3 pore by 1 μs atomistic molecular dynamic simulations. As PIPs are tetrameric pH gated channels we constructed homology MtPIP2,3 models in open and closed states, and with or without H2O2. All models were conformationally stable along the simulation and H2O2 permeation events were found in the simulations in the presence of this molecule. We find that: i- H2O2 molecules can cross the pore in a single file, iidihedral angles adopted by H2O2 along the pore Z axis present a different distribution compared to the angles visited in the solution; in the selectivity-determining NPA region, H2O2 adopts the wider range of dihedral angles, iii- higher residence times are located around the selectivity filter zone in the open channel and moves to the cytoplasmic filterarea in the closed channel; and iv- the constriction in the cytoplasmic filter area seems to be more stringent for H2O2 passage than for water.Our results shed light onto the molecular mechanism of H2O2 passage through MtPIP2,3 and represent the first steps to understand the structural determinants of AQP differential selectivity for these molecules and water.Fil: Chevriau, Jonathan. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Zerbetto de Palma, Gerardo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Zeida, Ari. Universidad de la República; UruguayFil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaXLIX Reunión Anual de la Sociedad Argentina de BiofísicaArgentinaSociedad Argentina de BiofisicaSociedad Argentina de Biofisica2021info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/196878Mechanistics insights of hydrogen peroxide transport through PIP aquaporins pore; XLIX Reunión Anual de la Sociedad Argentina de Biofísica; Argentina; 2021; 119-119978-987-27591-9-3CONICET DigitalCONICETengNacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:47:36Zoai:ri.conicet.gov.ar:11336/196878instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:47:36.395CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Mechanistics insights of hydrogen peroxide transport through PIP aquaporins pore
title Mechanistics insights of hydrogen peroxide transport through PIP aquaporins pore
spellingShingle Mechanistics insights of hydrogen peroxide transport through PIP aquaporins pore
Chevriau, Jonathan
ACUAPORINAS
PEROXIDO DE HIDROGENO
TRANSPORTE
title_short Mechanistics insights of hydrogen peroxide transport through PIP aquaporins pore
title_full Mechanistics insights of hydrogen peroxide transport through PIP aquaporins pore
title_fullStr Mechanistics insights of hydrogen peroxide transport through PIP aquaporins pore
title_full_unstemmed Mechanistics insights of hydrogen peroxide transport through PIP aquaporins pore
title_sort Mechanistics insights of hydrogen peroxide transport through PIP aquaporins pore
dc.creator.none.fl_str_mv Chevriau, Jonathan
Zerbetto de Palma, Gerardo Gabriel
Zeida, Ari
Alleva, Karina Edith
author Chevriau, Jonathan
author_facet Chevriau, Jonathan
Zerbetto de Palma, Gerardo Gabriel
Zeida, Ari
Alleva, Karina Edith
author_role author
author2 Zerbetto de Palma, Gerardo Gabriel
Zeida, Ari
Alleva, Karina Edith
author2_role author
author
author
dc.subject.none.fl_str_mv ACUAPORINAS
PEROXIDO DE HIDROGENO
TRANSPORTE
topic ACUAPORINAS
PEROXIDO DE HIDROGENO
TRANSPORTE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Hydrogen peroxide (H2O2) is transported through membranes by aquaporins (AQP). In particular, some plant PIP aquaporins isoforms are efficient H2O2 channels. As water and H2O2 share physicochemical features, it was first supposed that all AQP that transport water could act as an H2O2 channel. However, experimental evidence showed that not all PIP that transport water can transport H2O2. So, the mechanism of H2O2 transport is still an unsolved issue for AQP channels. MtPIP2,3 is a plasma membrane AQP from the legume Medicago truncatula that permeates H2O2. To understand the structural and chemical selectivity mechanisms leading to H2O2 permeability in PIPs, we characterized the particularities of H2O2 passingthrough MtPIP2,3 pore by 1 μs atomistic molecular dynamic simulations. As PIPs are tetrameric pH gated channels we constructed homology MtPIP2,3 models in open and closed states, and with or without H2O2. All models were conformationally stable along the simulation and H2O2 permeation events were found in the simulations in the presence of this molecule. We find that: i- H2O2 molecules can cross the pore in a single file, iidihedral angles adopted by H2O2 along the pore Z axis present a different distribution compared to the angles visited in the solution; in the selectivity-determining NPA region, H2O2 adopts the wider range of dihedral angles, iii- higher residence times are located around the selectivity filter zone in the open channel and moves to the cytoplasmic filterarea in the closed channel; and iv- the constriction in the cytoplasmic filter area seems to be more stringent for H2O2 passage than for water.Our results shed light onto the molecular mechanism of H2O2 passage through MtPIP2,3 and represent the first steps to understand the structural determinants of AQP differential selectivity for these molecules and water.
Fil: Chevriau, Jonathan. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Zerbetto de Palma, Gerardo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Zeida, Ari. Universidad de la República; Uruguay
Fil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
XLIX Reunión Anual de la Sociedad Argentina de Biofísica
Argentina
Sociedad Argentina de Biofisica
description Hydrogen peroxide (H2O2) is transported through membranes by aquaporins (AQP). In particular, some plant PIP aquaporins isoforms are efficient H2O2 channels. As water and H2O2 share physicochemical features, it was first supposed that all AQP that transport water could act as an H2O2 channel. However, experimental evidence showed that not all PIP that transport water can transport H2O2. So, the mechanism of H2O2 transport is still an unsolved issue for AQP channels. MtPIP2,3 is a plasma membrane AQP from the legume Medicago truncatula that permeates H2O2. To understand the structural and chemical selectivity mechanisms leading to H2O2 permeability in PIPs, we characterized the particularities of H2O2 passingthrough MtPIP2,3 pore by 1 μs atomistic molecular dynamic simulations. As PIPs are tetrameric pH gated channels we constructed homology MtPIP2,3 models in open and closed states, and with or without H2O2. All models were conformationally stable along the simulation and H2O2 permeation events were found in the simulations in the presence of this molecule. We find that: i- H2O2 molecules can cross the pore in a single file, iidihedral angles adopted by H2O2 along the pore Z axis present a different distribution compared to the angles visited in the solution; in the selectivity-determining NPA region, H2O2 adopts the wider range of dihedral angles, iii- higher residence times are located around the selectivity filter zone in the open channel and moves to the cytoplasmic filterarea in the closed channel; and iv- the constriction in the cytoplasmic filter area seems to be more stringent for H2O2 passage than for water.Our results shed light onto the molecular mechanism of H2O2 passage through MtPIP2,3 and represent the first steps to understand the structural determinants of AQP differential selectivity for these molecules and water.
publishDate 2021
dc.date.none.fl_str_mv 2021
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Reunión
Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/196878
Mechanistics insights of hydrogen peroxide transport through PIP aquaporins pore; XLIX Reunión Anual de la Sociedad Argentina de Biofísica; Argentina; 2021; 119-119
978-987-27591-9-3
CONICET Digital
CONICET
url http://hdl.handle.net/11336/196878
identifier_str_mv Mechanistics insights of hydrogen peroxide transport through PIP aquaporins pore; XLIX Reunión Anual de la Sociedad Argentina de Biofísica; Argentina; 2021; 119-119
978-987-27591-9-3
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Sociedad Argentina de Biofisica
publisher.none.fl_str_mv Sociedad Argentina de Biofisica
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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