TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.

Autores
Fabiani, Camila; Georgiev, V.; Dimova. R.; Antollini, Silvia Susana
Año de publicación
2021
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Nicotinic acetylcholine receptors (nAChRs) are integral membrane pentameric proteins that belong to the Cys-loop superfamily of ligand-gated ion channels. Given that the nAChR is a transmembrane protein, the properties of the membrane where it is embedded are essential for its correct functioning, and since even small changes in nAChRs activity can cause great effects on human biology, the interaction between lipids and the nAChR is of great relevance. The transmembrane domain of each subunit of the nAChR is composed of four segments (TM1-TM4) in which TM2 segments form the ion channel pore and TM1, TM3, and TM4 are located more externally. TM4 segment is the most exposed and it isin intimate contact with both the surrounding membrane lipids and the rest of the transmembrane segments, these being two facts that make it a key participant in lipid- nAChR interaction.Due to the abundance of Chol in neural membranes and its importance and implication in different human diseases, in this work we studied the relationship between domains either rich in cholesterol (Liquid order domains, Lo) or poor in cholesterol (Liquid disorder domains, Ld) and the nAChR. To this end, we worked with GUVs, giant unilamellar vesicles that can be observed under the microscope, formed by two different lipid compositions (with nanoscopic or microscopic Lo and Ld domains) containing or not a syntheticpeptide corresponding to the TM4 segment of the nAChR.Confocal Fluorescence Microscopy, Fluorescence Recovery After Photobleaching (FRAP) measurements and experiments of Miscibility Transition Temperature showed that TM4 peptide concentrates in Ld domains. Furthermore, we observed that its presence alters the intrinsic properties of the domains as well as the whole microscopic membrane organization. It is well known that lipids condition nAChR functioning, here we demonstrate that just this peptide, as a minimalist but still representative model of the nAChR, can perturb its lipid microenvironment as well.
Fil: Fabiani, Camila. 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
Fil: Georgiev, V.. Max Planck Institute Of Biochemistry.; Alemania
Fil: Dimova. R.. Max Planck Institute Of Biochemistry.; Alemania
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
XLIX Reunión Anual de la Sociedad Argentina de Biofísica
Buenos Aires
Argentina
Sociedad Argentina de Biofísica
Materia
nicotinic acetylcholine receptor
lipid domains
cholesterol
giant unilamellar vesicles
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:11336/229916
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/229916
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.Fabiani, CamilaGeorgiev, V.Dimova. R.Antollini, Silvia Susananicotinic acetylcholine receptorlipid domainscholesterolgiant unilamellar vesicleshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Nicotinic acetylcholine receptors (nAChRs) are integral membrane pentameric proteins that belong to the Cys-loop superfamily of ligand-gated ion channels. Given that the nAChR is a transmembrane protein, the properties of the membrane where it is embedded are essential for its correct functioning, and since even small changes in nAChRs activity can cause great effects on human biology, the interaction between lipids and the nAChR is of great relevance. The transmembrane domain of each subunit of the nAChR is composed of four segments (TM1-TM4) in which TM2 segments form the ion channel pore and TM1, TM3, and TM4 are located more externally. TM4 segment is the most exposed and it isin intimate contact with both the surrounding membrane lipids and the rest of the transmembrane segments, these being two facts that make it a key participant in lipid- nAChR interaction.Due to the abundance of Chol in neural membranes and its importance and implication in different human diseases, in this work we studied the relationship between domains either rich in cholesterol (Liquid order domains, Lo) or poor in cholesterol (Liquid disorder domains, Ld) and the nAChR. To this end, we worked with GUVs, giant unilamellar vesicles that can be observed under the microscope, formed by two different lipid compositions (with nanoscopic or microscopic Lo and Ld domains) containing or not a syntheticpeptide corresponding to the TM4 segment of the nAChR.Confocal Fluorescence Microscopy, Fluorescence Recovery After Photobleaching (FRAP) measurements and experiments of Miscibility Transition Temperature showed that TM4 peptide concentrates in Ld domains. Furthermore, we observed that its presence alters the intrinsic properties of the domains as well as the whole microscopic membrane organization. It is well known that lipids condition nAChR functioning, here we demonstrate that just this peptide, as a minimalist but still representative model of the nAChR, can perturb its lipid microenvironment as well.Fil: Fabiani, Camila. 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; ArgentinaFil: Georgiev, V.. Max Planck Institute Of Biochemistry.; AlemaniaFil: Dimova. R.. Max Planck Institute Of Biochemistry.; AlemaniaFil: 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; ArgentinaXLIX Reunión Anual de la Sociedad Argentina de BiofísicaBuenos AiresArgentinaSociedad Argentina de BiofísicaSociedad Argentina de Biofísica2021info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectCongresoBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/229916TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.; XLIX Reunión Anual de la Sociedad Argentina de Biofísica; Buenos Aires; Argentina; 2021; 66-66978-987-27591-9-3CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/Internacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:35:07Zoai:ri.conicet.gov.ar:11336/229916instacron: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 09:35:08.219CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.
title TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.
spellingShingle TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.
Fabiani, Camila
nicotinic acetylcholine receptor
lipid domains
cholesterol
giant unilamellar vesicles
title_short TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.
title_full TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.
title_fullStr TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.
title_full_unstemmed TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.
title_sort TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.
dc.creator.none.fl_str_mv Fabiani, Camila
Georgiev, V.
Dimova. R.
Antollini, Silvia Susana
author Fabiani, Camila
author_facet Fabiani, Camila
Georgiev, V.
Dimova. R.
Antollini, Silvia Susana
author_role author
author2 Georgiev, V.
Dimova. R.
Antollini, Silvia Susana
author2_role author
author
author
dc.subject.none.fl_str_mv nicotinic acetylcholine receptor
lipid domains
cholesterol
giant unilamellar vesicles
topic nicotinic acetylcholine receptor
lipid domains
cholesterol
giant unilamellar vesicles
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 integral membrane pentameric proteins that belong to the Cys-loop superfamily of ligand-gated ion channels. Given that the nAChR is a transmembrane protein, the properties of the membrane where it is embedded are essential for its correct functioning, and since even small changes in nAChRs activity can cause great effects on human biology, the interaction between lipids and the nAChR is of great relevance. The transmembrane domain of each subunit of the nAChR is composed of four segments (TM1-TM4) in which TM2 segments form the ion channel pore and TM1, TM3, and TM4 are located more externally. TM4 segment is the most exposed and it isin intimate contact with both the surrounding membrane lipids and the rest of the transmembrane segments, these being two facts that make it a key participant in lipid- nAChR interaction.Due to the abundance of Chol in neural membranes and its importance and implication in different human diseases, in this work we studied the relationship between domains either rich in cholesterol (Liquid order domains, Lo) or poor in cholesterol (Liquid disorder domains, Ld) and the nAChR. To this end, we worked with GUVs, giant unilamellar vesicles that can be observed under the microscope, formed by two different lipid compositions (with nanoscopic or microscopic Lo and Ld domains) containing or not a syntheticpeptide corresponding to the TM4 segment of the nAChR.Confocal Fluorescence Microscopy, Fluorescence Recovery After Photobleaching (FRAP) measurements and experiments of Miscibility Transition Temperature showed that TM4 peptide concentrates in Ld domains. Furthermore, we observed that its presence alters the intrinsic properties of the domains as well as the whole microscopic membrane organization. It is well known that lipids condition nAChR functioning, here we demonstrate that just this peptide, as a minimalist but still representative model of the nAChR, can perturb its lipid microenvironment as well.
Fil: Fabiani, Camila. 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
Fil: Georgiev, V.. Max Planck Institute Of Biochemistry.; Alemania
Fil: Dimova. R.. Max Planck Institute Of Biochemistry.; Alemania
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
XLIX Reunión Anual de la Sociedad Argentina de Biofísica
Buenos Aires
Argentina
Sociedad Argentina de Biofísica
description Nicotinic acetylcholine receptors (nAChRs) are integral membrane pentameric proteins that belong to the Cys-loop superfamily of ligand-gated ion channels. Given that the nAChR is a transmembrane protein, the properties of the membrane where it is embedded are essential for its correct functioning, and since even small changes in nAChRs activity can cause great effects on human biology, the interaction between lipids and the nAChR is of great relevance. The transmembrane domain of each subunit of the nAChR is composed of four segments (TM1-TM4) in which TM2 segments form the ion channel pore and TM1, TM3, and TM4 are located more externally. TM4 segment is the most exposed and it isin intimate contact with both the surrounding membrane lipids and the rest of the transmembrane segments, these being two facts that make it a key participant in lipid- nAChR interaction.Due to the abundance of Chol in neural membranes and its importance and implication in different human diseases, in this work we studied the relationship between domains either rich in cholesterol (Liquid order domains, Lo) or poor in cholesterol (Liquid disorder domains, Ld) and the nAChR. To this end, we worked with GUVs, giant unilamellar vesicles that can be observed under the microscope, formed by two different lipid compositions (with nanoscopic or microscopic Lo and Ld domains) containing or not a syntheticpeptide corresponding to the TM4 segment of the nAChR.Confocal Fluorescence Microscopy, Fluorescence Recovery After Photobleaching (FRAP) measurements and experiments of Miscibility Transition Temperature showed that TM4 peptide concentrates in Ld domains. Furthermore, we observed that its presence alters the intrinsic properties of the domains as well as the whole microscopic membrane organization. It is well known that lipids condition nAChR functioning, here we demonstrate that just this peptide, as a minimalist but still representative model of the nAChR, can perturb its lipid microenvironment as well.
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
Congreso
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/11336/229916
TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.; XLIX Reunión Anual de la Sociedad Argentina de Biofísica; Buenos Aires; Argentina; 2021; 66-66
978-987-27591-9-3
CONICET Digital
CONICET
url http://hdl.handle.net/11336/229916
identifier_str_mv TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.; XLIX Reunión Anual de la Sociedad Argentina de Biofísica; Buenos Aires; Argentina; 2021; 66-66
978-987-27591-9-3
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 Internacional
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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