Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayers

Autores
Pissinis, Diego Ezequiel; Díaz, Carolina; Maza, Eliana María; Bonini, Ida C.; Barrantes, Francisco J.; Salvarezza, Roberto Carlos; Schilardi, Patricia Laura
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The insertion and function of the muscle-type nicotinic acetylcholine receptor (nAChR) in Au(111)- supported thiolipid self-assembled monolayers have been studied by atomic force microscopy (AFM), surface plasmon resonance (SPR), and electrochemical techniques. It was possible for the first time to resolve the supramolecular arrangement of the protein spontaneously inserted in a thiolipid monolayer in an aqueous solution. Geometric supramolecular arrays of nAChRs were observed, most commonly in a triangular form compatible with three nAChR dimers of ∼20 nm each. Addition of the full agonist carbamoylcholine activated and opened the nAChR ion channel, as revealed by the increase in capacitance relative to that of the nAChR–thiolipid system under basal conditions. Thus, the self-assembled system appears to be a viable biomimetic model to measure ionic conductance mediated by ion-gated ion channels under different experimental conditions, with potential applications in biotechnology and pharmacology.
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
Materia
Química
Física
nicotinic acetylcholine receptor
atomic force microscopy
surface plasmon resonance
electrochemical techniques
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/147632
Acceder
id SEDICI_4c04612101a1d3c9088cda356190eb99
oai_identifier_str oai:sedici.unlp.edu.ar:10915/147632
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayersPissinis, Diego EzequielDíaz, CarolinaMaza, Eliana MaríaBonini, Ida C.Barrantes, Francisco J.Salvarezza, Roberto CarlosSchilardi, Patricia LauraQuímicaFísicanicotinic acetylcholine receptoratomic force microscopysurface plasmon resonanceelectrochemical techniquesThe insertion and function of the muscle-type nicotinic acetylcholine receptor (nAChR) in Au(111)- supported thiolipid self-assembled monolayers have been studied by atomic force microscopy (AFM), surface plasmon resonance (SPR), and electrochemical techniques. It was possible for the first time to resolve the supramolecular arrangement of the protein spontaneously inserted in a thiolipid monolayer in an aqueous solution. Geometric supramolecular arrays of nAChRs were observed, most commonly in a triangular form compatible with three nAChR dimers of ∼20 nm each. Addition of the full agonist carbamoylcholine activated and opened the nAChR ion channel, as revealed by the increase in capacitance relative to that of the nAChR–thiolipid system under basal conditions. Thus, the self-assembled system appears to be a viable biomimetic model to measure ionic conductance mediated by ion-gated ion channels under different experimental conditions, with potential applications in biotechnology and pharmacology.Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas2015info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf15789-15797http://sedici.unlp.edu.ar/handle/10915/147632enginfo:eu-repo/semantics/altIdentifier/issn/2040-3364info:eu-repo/semantics/altIdentifier/issn/2040-3372info:eu-repo/semantics/altIdentifier/doi/10.1039/c5nr04109kinfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-22T17:18:36Zoai:sedici.unlp.edu.ar:10915/147632Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-22 17:18:37.167SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayers
title Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayers
spellingShingle Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayers
Pissinis, Diego Ezequiel
Química
Física
nicotinic acetylcholine receptor
atomic force microscopy
surface plasmon resonance
electrochemical techniques
title_short Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayers
title_full Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayers
title_fullStr Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayers
title_full_unstemmed Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayers
title_sort Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayers
dc.creator.none.fl_str_mv Pissinis, Diego Ezequiel
Díaz, Carolina
Maza, Eliana María
Bonini, Ida C.
Barrantes, Francisco J.
Salvarezza, Roberto Carlos
Schilardi, Patricia Laura
author Pissinis, Diego Ezequiel
author_facet Pissinis, Diego Ezequiel
Díaz, Carolina
Maza, Eliana María
Bonini, Ida C.
Barrantes, Francisco J.
Salvarezza, Roberto Carlos
Schilardi, Patricia Laura
author_role author
author2 Díaz, Carolina
Maza, Eliana María
Bonini, Ida C.
Barrantes, Francisco J.
Salvarezza, Roberto Carlos
Schilardi, Patricia Laura
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Química
Física
nicotinic acetylcholine receptor
atomic force microscopy
surface plasmon resonance
electrochemical techniques
topic Química
Física
nicotinic acetylcholine receptor
atomic force microscopy
surface plasmon resonance
electrochemical techniques
dc.description.none.fl_txt_mv The insertion and function of the muscle-type nicotinic acetylcholine receptor (nAChR) in Au(111)- supported thiolipid self-assembled monolayers have been studied by atomic force microscopy (AFM), surface plasmon resonance (SPR), and electrochemical techniques. It was possible for the first time to resolve the supramolecular arrangement of the protein spontaneously inserted in a thiolipid monolayer in an aqueous solution. Geometric supramolecular arrays of nAChRs were observed, most commonly in a triangular form compatible with three nAChR dimers of ∼20 nm each. Addition of the full agonist carbamoylcholine activated and opened the nAChR ion channel, as revealed by the increase in capacitance relative to that of the nAChR–thiolipid system under basal conditions. Thus, the self-assembled system appears to be a viable biomimetic model to measure ionic conductance mediated by ion-gated ion channels under different experimental conditions, with potential applications in biotechnology and pharmacology.
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
description The insertion and function of the muscle-type nicotinic acetylcholine receptor (nAChR) in Au(111)- supported thiolipid self-assembled monolayers have been studied by atomic force microscopy (AFM), surface plasmon resonance (SPR), and electrochemical techniques. It was possible for the first time to resolve the supramolecular arrangement of the protein spontaneously inserted in a thiolipid monolayer in an aqueous solution. Geometric supramolecular arrays of nAChRs were observed, most commonly in a triangular form compatible with three nAChR dimers of ∼20 nm each. Addition of the full agonist carbamoylcholine activated and opened the nAChR ion channel, as revealed by the increase in capacitance relative to that of the nAChR–thiolipid system under basal conditions. Thus, the self-assembled system appears to be a viable biomimetic model to measure ionic conductance mediated by ion-gated ion channels under different experimental conditions, with potential applications in biotechnology and pharmacology.
publishDate 2015
dc.date.none.fl_str_mv 2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/147632
url http://sedici.unlp.edu.ar/handle/10915/147632
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/2040-3364
info:eu-repo/semantics/altIdentifier/issn/2040-3372
info:eu-repo/semantics/altIdentifier/doi/10.1039/c5nr04109k
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
15789-15797
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 12.982451

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