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dc.contributor.author
Herrera, Maria Georgina
dc.contributor.author
Gomez Castro, Maria Florencia
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Prieto, Eduardo Daniel
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Barrera Guisasola, Exequiel Ernesto
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Dodero, Veronica Isabel
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Pantano Gutierrez, Sergio Fabian
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Chirdo, Fernando Gabriel
dc.date.available
2020-11-19T18:29:17Z
dc.date.issued
2019-10
dc.identifier.citation
Herrera, Maria Georgina; Gomez Castro, Maria Florencia; Prieto, Eduardo Daniel; Barrera Guisasola, Exequiel Ernesto; Dodero, Veronica Isabel; et al.; Structural conformation and self‐assembly process of p31‐43 gliadin peptide in aqueous solution. Implications for celiac disease; Wiley Blackwell Publishing, Inc; Febs Journal; 287; 10; 10-2019; 2134-2149
dc.identifier.issn
1742-464X
dc.identifier.uri
http://hdl.handle.net/11336/118665
dc.description.abstract
Celiac Disease (CeD) is a highly prevalent chronic immune-mediated enteropathy developed in genetically predisposed individuals after ingestion of a group of wheat proteins (called gliadins and glutenins). The 13mer α-gliadin peptide, p31-43, induces proinflammatory responses, observed by in vitro assays and animal models, that may contribute to innate immune mechanisms of CeD pathogenesis. Since a cellular receptor for p31-43 has not been identified, this raises the question of whether this peptide could mediate different biological effects. In this work, we aimed to characterize the p31-43 secondary structure by different biophysical and in silico techniques. By Dynamic Light Scattering (DLS) and using an oligomer/fibril-sensitive fluorescent probe, we showed the presence of oligomers of this peptide in solution. Furthermore, Atomic Force Microscopy (AFM) analysis showed p31-43 oligomers with different height distribution. Also, peptide concentration had a very strong influence on peptide self-organization process. Oligomers gradually increased their size at lower concentration. Whereas, at higher ones, oligomers increased their complexity, forming branched structures. By Circular Dichroism, we observed that p31-43 self-organized in a poly-proline II conformation in equilibrium with βsheets-like structures, whose pH remained stable in the range of 3 to 8. In addition, these findings were supported by Molecular Dynamics Simulation. The formation of p31-43 nanostructures with increased β-sheet structure may help to explain the molecular etiopathogenesis in the induction of pro-inflammatory effects and subsequent damage at the intestinal mucosa in CeD.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley Blackwell Publishing, Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
CELIAC DISEASE
dc.subject
GLIADIN P31-43 PEPTIDE
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OLIGOMERS
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SECONDARY STRUCTURE
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Biofísica
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Structural conformation and self‐assembly process of p31‐43 gliadin peptide in aqueous solution. Implications for celiac disease
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-11-17T16:38:04Z
dc.journal.volume
287
dc.journal.number
10
dc.journal.pagination
2134-2149
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Herrera, Maria Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.description.fil
Fil: Gomez Castro, Maria Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Estudios Inmunológicos y Fisiopatológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Estudios Inmunológicos y Fisiopatológicos; Argentina
dc.description.fil
Fil: Prieto, Eduardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina
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Fil: Barrera Guisasola, Exequiel Ernesto. Instituto Pasteur de Montevideo; Uruguay. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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Fil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania
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Fil: Pantano Gutierrez, Sergio Fabian. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Chirdo, Fernando Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Estudios Inmunológicos y Fisiopatológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Estudios Inmunológicos y Fisiopatológicos; Argentina
dc.journal.title
Febs Journal
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/febs.15109
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1111/febs.15109
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