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dc.contributor.author
Antollini, Silvia Susana
dc.contributor.author
Xue, Yechun
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Jiang, Hualiang
dc.contributor.author
Barrantes, Francisco Jose
dc.date.available
2018-05-02T15:30:51Z
dc.date.issued
2009-07-09
dc.identifier.citation
Antollini, Silvia Susana; Xue, Yechun; Jiang, Hualiang; Barrantes, Francisco Jose; Fluorescence and molecular dynamics studies of the acetylcholine receptor γM4 transmembrane peptide in reconstituted systems; Taylor & Francis Ltd; Molecular Membrane Biology; 22; 6; 9-7-2009; 471-483
dc.identifier.issn
0968-7688
dc.identifier.uri
http://hdl.handle.net/11336/43845
dc.description.abstract
A combination of fluorescence spectroscopy and molecular dynamics (MD) is applied to assess the conformational dynamics of a peptide making up the outermost ring of the nicotinic acetylcholine receptor (AChR) transmembrane region and the effect of membrane thickness and cholesterol on the hydrophobic matching of this peptide. The fluorescence studies exploit the intrinsic fluorescence of the only tryptophan residue in a synthetic peptide corresponding to the fourth transmembrane domain of the AChR γ subunit (γM4-Trp6) reconstituted in lipid bilayers of varying thickness, and combine this information with quenching studies using depth-sensitive phosphatidylcholine spin-labeled probes and acrylamide, polarization of fluorescence, and generalized polarization of Laurdan. A direct correlation was found between bilayer width and the depth of insertion of Trp6. We further extend our recent MD study of the conformational dynamics of the AChR channel to focus on the crosstalk between M4 and the lipid-belt region. The isolated γM4 peptide is shown to possess considerable orientational flexibility while maintaining a linear α-helical structure, and to vary its tilt depending on bilayer width and cholesterol (Chol) content. MD studies also show that γM4 also establishes contacts with the other TM peptides on its inner face, stabilizing a shorter TM length that is still highly sensitive to the lipid environment. In the native membrane the topology of the M4 ring is likely to exhibit a similar behavior, dynamically modifying its tilt to match the hydrophobic thickness of the bilayer.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Taylor & Francis Ltd
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Achr
dc.subject
Fluorescencia
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Fluorescence and molecular dynamics studies of the acetylcholine receptor γM4 transmembrane peptide in reconstituted systems
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-04-18T15:09:19Z
dc.identifier.eissn
1464-5203
dc.journal.volume
22
dc.journal.number
6
dc.journal.pagination
471-483
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
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. Unesco; Argentina
dc.description.fil
Fil: Xue, Yechun. Shanghai Institute for Biological Sciences; China
dc.description.fil
Fil: Jiang, Hualiang. Shanghai Institute for Biological Sciences; China. East.China University of Science and Technology. School of Pharmacy; China
dc.description.fil
Fil: Barrantes, Francisco Jose. 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. Unesco; Argentina
dc.journal.title
Molecular Membrane Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/full/10.1080/09687860500367915
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1080/09687860500367915
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