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

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...

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Autores principales: Pissinis, Diego Ezequiel, Díaz, Carolina, Maza, Eliana María, Bonini, Ida C., Barrantes, Francisco J., Salvarezza, Roberto Carlos, Schilardi, Patricia Laura
Formato: Articulo
Lenguaje:Inglés
Publicado: 2015
Materias:
Química
Física
nicotinic acetylcholine receptor
atomic force microscopy
surface plasmon resonance
electrochemical techniques
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/147632
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-147632
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Química
Física
nicotinic acetylcholine receptor
atomic force microscopy
surface plasmon resonance
electrochemical techniques
spellingShingle Química
Física
nicotinic acetylcholine receptor
atomic force microscopy
surface plasmon resonance
electrochemical techniques
Pissinis, Diego Ezequiel
Díaz, Carolina
Maza, Eliana María
Bonini, Ida C.
Barrantes, Francisco J.
Salvarezza, Roberto Carlos
Schilardi, Patricia Laura
Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayers
topic_facet Química
Física
nicotinic acetylcholine receptor
atomic force microscopy
surface plasmon resonance
electrochemical techniques
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.
format Articulo
Articulo
author Pissinis, Diego Ezequiel
Díaz, Carolina
Maza, Eliana María
Bonini, Ida C.
Barrantes, Francisco J.
Salvarezza, Roberto Carlos
Schilardi, Patricia Laura
author_facet Pissinis, Diego Ezequiel
Díaz, Carolina
Maza, Eliana María
Bonini, Ida C.
Barrantes, Francisco J.
Salvarezza, Roberto Carlos
Schilardi, Patricia Laura
author_sort Pissinis, Diego Ezequiel
title Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayers
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
publishDate 2015
url http://sedici.unlp.edu.ar/handle/10915/147632
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