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dc.contributor.author
Fabiani, Camila
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dc.contributor.author
Georgiev, V.
dc.contributor.author
Dimova. R.
dc.contributor.author
Antollini, Silvia Susana
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dc.date.available
2024-03-11T09:42:14Z
dc.date.issued
2021
dc.identifier.citation
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
dc.identifier.isbn
978-987-27591-9-3
dc.identifier.uri
http://hdl.handle.net/11336/229916
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Sociedad Argentina de Biofísica
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
nicotinic acetylcholine receptor
dc.subject
lipid domains
dc.subject
cholesterol
dc.subject
giant unilamellar vesicles
dc.subject.classification
Biofísica
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
TM4 peptide, as a representative model of the AChR, conditions its lipid microenvironment.
dc.type
info:eu-repo/semantics/publishedVersion
dc.type
info:eu-repo/semantics/conferenceObject
dc.type
info:ar-repo/semantics/documento de conferencia
dc.date.updated
2024-02-22T14:25:59Z
dc.journal.pagination
66-66
dc.journal.pais
Argentina
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dc.journal.ciudad
Buenos Aires
dc.description.fil
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
dc.description.fil
Fil: Georgiev, V.. Max Planck Institute Of Biochemistry.; Alemania
dc.description.fil
Fil: Dimova. R.. Max Planck Institute Of Biochemistry.; Alemania
dc.description.fil
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
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/
dc.conicet.rol
Autor
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Autor
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dc.conicet.rol
Autor
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dc.conicet.rol
Autor
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dc.coverage
Internacional
dc.type.subtype
Congreso
dc.description.nombreEvento
XLIX Reunión Anual de la Sociedad Argentina de Biofísica
dc.date.evento
2021-12-01
dc.description.ciudadEvento
Buenos Aires
dc.description.paisEvento
Argentina
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dc.type.publicacion
Book
dc.description.institucionOrganizadora
Sociedad Argentina de Biofísica
dc.source.libro
XLIX Reunión Anual de la Sociedad Argentina de Biofísica
dc.date.eventoHasta
2021-12-03
dc.type
Congreso
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