Cholesterol effects on α7-nAChR embedded in POPC bilayer

Autores
Vietri, Agustin; Obiol, Diego Javier; Amundarain, María Julia; Zamarreño, Fernando; Antollini, Silvia Susana; Costabel, M.
Año de publicación
2022
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels (LGIC) made up of five transmembrane glycoprotein subunits organized pseudosymmetrically around a central pore or channel. They can adopt three main conformational states, in addition to several other intermediate states: a closed (C) or resting (R) state, an open (O) state that occurs after agonist binding, and a desensitized (D) state that occurs after the continued presence of the agonist. Subtle changes in the lipid environment of the nAChRs have great relevance in their activity, causing significant effects on human biology. Two types of lipid positions can be identified for these lipids: annular and non-annular. Non-annular sites are in close contact with the receptor and have a low replacement rate, while the annular ones are further away, with a higher replacement rate. In this work, we use a receptor model based on a known structure (PDB: 7EKI) inserted in a lipid bilayer composed entirely of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) lipids. Lipids at annular sites of the membrane were replaced by cholesterols, obtaining different lipid environments for the receptor. Atomistic Molecular Dynamics were performed for the receptor and the membrane with various combinations of these cholesterols. Physicochemical properties of the membrane and the receptor were analyzed and compared with the results obtained for the control system, which lacks cholesterol molecules.
Fil: Vietri, Agustin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Obiol, Diego Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Amundarain, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Zamarreño, Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Antollini, Silvia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina
Fil: Costabel, M.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
L Reunión Anual de la Sociedad Argentina de Biofísica
Rosario
Argentina
Sociedad Argentina de Biofísica
Materia
nicotinic acetylcholine receptor
cholesterol
lipid-membrane interactions
Atomistic Molecular Dynamics
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:11336/225296
Acceder
id CONICETDig_f4dda687c81045583c194d90654f941d
oai_identifier_str oai:ri.conicet.gov.ar:11336/225296
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Cholesterol effects on α7-nAChR embedded in POPC bilayerVietri, AgustinObiol, Diego JavierAmundarain, María JuliaZamarreño, FernandoAntollini, Silvia SusanaCostabel, M.nicotinic acetylcholine receptorcholesterollipid-membrane interactionsAtomistic Molecular Dynamicshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels (LGIC) made up of five transmembrane glycoprotein subunits organized pseudosymmetrically around a central pore or channel. They can adopt three main conformational states, in addition to several other intermediate states: a closed (C) or resting (R) state, an open (O) state that occurs after agonist binding, and a desensitized (D) state that occurs after the continued presence of the agonist. Subtle changes in the lipid environment of the nAChRs have great relevance in their activity, causing significant effects on human biology. Two types of lipid positions can be identified for these lipids: annular and non-annular. Non-annular sites are in close contact with the receptor and have a low replacement rate, while the annular ones are further away, with a higher replacement rate. In this work, we use a receptor model based on a known structure (PDB: 7EKI) inserted in a lipid bilayer composed entirely of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) lipids. Lipids at annular sites of the membrane were replaced by cholesterols, obtaining different lipid environments for the receptor. Atomistic Molecular Dynamics were performed for the receptor and the membrane with various combinations of these cholesterols. Physicochemical properties of the membrane and the receptor were analyzed and compared with the results obtained for the control system, which lacks cholesterol molecules.Fil: Vietri, Agustin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; ArgentinaFil: Obiol, Diego Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; ArgentinaFil: Amundarain, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; ArgentinaFil: Zamarreño, Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; ArgentinaFil: Antollini, Silvia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; ArgentinaFil: Costabel, M.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; ArgentinaL Reunión Anual de la Sociedad Argentina de BiofísicaRosarioArgentinaSociedad Argentina de BiofísicaSociedad Argentina de Biofísica2022info: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/11336/225296Cholesterol effects on α7-nAChR embedded in POPC bilayer; L Reunión Anual de la Sociedad Argentina de Biofísica; Rosario; Argentina; 2022; 44-44978-987-48938-0-2CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/Nacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:59:44Zoai:ri.conicet.gov.ar:11336/225296instacron: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 09:59:45.247CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Cholesterol effects on α7-nAChR embedded in POPC bilayer
title Cholesterol effects on α7-nAChR embedded in POPC bilayer
spellingShingle Cholesterol effects on α7-nAChR embedded in POPC bilayer
Vietri, Agustin
nicotinic acetylcholine receptor
cholesterol
lipid-membrane interactions
Atomistic Molecular Dynamics
title_short Cholesterol effects on α7-nAChR embedded in POPC bilayer
title_full Cholesterol effects on α7-nAChR embedded in POPC bilayer
title_fullStr Cholesterol effects on α7-nAChR embedded in POPC bilayer
title_full_unstemmed Cholesterol effects on α7-nAChR embedded in POPC bilayer
title_sort Cholesterol effects on α7-nAChR embedded in POPC bilayer
dc.creator.none.fl_str_mv Vietri, Agustin
Obiol, Diego Javier
Amundarain, María Julia
Zamarreño, Fernando
Antollini, Silvia Susana
Costabel, M.
author Vietri, Agustin
author_facet Vietri, Agustin
Obiol, Diego Javier
Amundarain, María Julia
Zamarreño, Fernando
Antollini, Silvia Susana
Costabel, M.
author_role author
author2 Obiol, Diego Javier
Amundarain, María Julia
Zamarreño, Fernando
Antollini, Silvia Susana
Costabel, M.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv nicotinic acetylcholine receptor
cholesterol
lipid-membrane interactions
Atomistic Molecular Dynamics
topic nicotinic acetylcholine receptor
cholesterol
lipid-membrane interactions
Atomistic Molecular Dynamics
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels (LGIC) made up of five transmembrane glycoprotein subunits organized pseudosymmetrically around a central pore or channel. They can adopt three main conformational states, in addition to several other intermediate states: a closed (C) or resting (R) state, an open (O) state that occurs after agonist binding, and a desensitized (D) state that occurs after the continued presence of the agonist. Subtle changes in the lipid environment of the nAChRs have great relevance in their activity, causing significant effects on human biology. Two types of lipid positions can be identified for these lipids: annular and non-annular. Non-annular sites are in close contact with the receptor and have a low replacement rate, while the annular ones are further away, with a higher replacement rate. In this work, we use a receptor model based on a known structure (PDB: 7EKI) inserted in a lipid bilayer composed entirely of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) lipids. Lipids at annular sites of the membrane were replaced by cholesterols, obtaining different lipid environments for the receptor. Atomistic Molecular Dynamics were performed for the receptor and the membrane with various combinations of these cholesterols. Physicochemical properties of the membrane and the receptor were analyzed and compared with the results obtained for the control system, which lacks cholesterol molecules.
Fil: Vietri, Agustin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Obiol, Diego Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Amundarain, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Zamarreño, Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Antollini, Silvia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina
Fil: Costabel, M.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
L Reunión Anual de la Sociedad Argentina de Biofísica
Rosario
Argentina
Sociedad Argentina de Biofísica
description Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels (LGIC) made up of five transmembrane glycoprotein subunits organized pseudosymmetrically around a central pore or channel. They can adopt three main conformational states, in addition to several other intermediate states: a closed (C) or resting (R) state, an open (O) state that occurs after agonist binding, and a desensitized (D) state that occurs after the continued presence of the agonist. Subtle changes in the lipid environment of the nAChRs have great relevance in their activity, causing significant effects on human biology. Two types of lipid positions can be identified for these lipids: annular and non-annular. Non-annular sites are in close contact with the receptor and have a low replacement rate, while the annular ones are further away, with a higher replacement rate. In this work, we use a receptor model based on a known structure (PDB: 7EKI) inserted in a lipid bilayer composed entirely of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) lipids. Lipids at annular sites of the membrane were replaced by cholesterols, obtaining different lipid environments for the receptor. Atomistic Molecular Dynamics were performed for the receptor and the membrane with various combinations of these cholesterols. Physicochemical properties of the membrane and the receptor were analyzed and compared with the results obtained for the control system, which lacks cholesterol molecules.
publishDate 2022
dc.date.none.fl_str_mv 2022
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/11336/225296
Cholesterol effects on α7-nAChR embedded in POPC bilayer; L Reunión Anual de la Sociedad Argentina de Biofísica; Rosario; Argentina; 2022; 44-44
978-987-48938-0-2
CONICET Digital
CONICET
url http://hdl.handle.net/11336/225296
identifier_str_mv Cholesterol effects on α7-nAChR embedded in POPC bilayer; L Reunión Anual de la Sociedad Argentina de Biofísica; Rosario; Argentina; 2022; 44-44
978-987-48938-0-2
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/
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 Biofísica
publisher.none.fl_str_mv Sociedad Argentina de Biofísica
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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