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dc.contributor.author
Herrera, Maria Georgina

dc.contributor.author
Dodero, Veronica Isabel

dc.date.available
2022-07-18T11:11:40Z
dc.date.issued
2021-12
dc.identifier.citation
Herrera, Maria Georgina; Dodero, Veronica Isabel; Gliadin proteolytical resistant peptides: the interplay between structure and self-assembly in gluten-related disorders; Springer; Biophysical Reviews; 13; 6; 12-2021; 1147-1154
dc.identifier.issn
1867-2450
dc.identifier.uri
http://hdl.handle.net/11336/162285
dc.description.abstract
In recent years, the evaluation of the structural properties of food has become of crucial importance in the understanding of food-related disorders. One of the most exciting systems is gliadin, a protein in wheat gluten, that plays a protagonist role in gluten-related disorders with a worldwide prevalence of 5%, including autoimmune celiac disease (CeD) (1%) and non-celiac wheat sensitivity (0.5–13%). It is accepted that gliadin is not fully digested by humans, producing large peptides that reach the gut mucosa. The gliadin peptides cross the lamina propria eliciting different immune responses in susceptible patients. Many clinical and biomedical efforts aim to diagnose and understand gluten-related disorders; meanwhile, the early stages of the inflammatory events remain elusive. Interestingly, although the primary sequence of many gliadin peptides is well known, it was only recently revealed the self-assembly capability of two pathogenic gliadin fragments and their connection to the early stage of diseases. This review is dedicated to the most relevant biophysical characterization of the complex gliadin digest and the two most studied gliadin fragments, the immunodominant 33-mer peptide and the toxic p31-43 in connection with inflammation and innate immune response. Here, we want to emphasize that combining different biophysical methods with cellular and in vivo models is of key importance to get an integrative understanding of a complex biological problem, as discussed here.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer

dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
GLUTEN-RELATED DISORDERS
dc.subject
MICROSCOPIES
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SECONDARY STRUCTURE
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SELF-ASSEMBLY
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SPECTROSCOPIC METHODS
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Biofísica

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Ciencias Biológicas

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CIENCIAS NATURALES Y EXACTAS

dc.title
Gliadin proteolytical resistant peptides: the interplay between structure and self-assembly in gluten-related disorders
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2022-07-15T14:47:16Z
dc.identifier.eissn
1867-2469
dc.journal.volume
13
dc.journal.number
6
dc.journal.pagination
1147-1154
dc.journal.pais
Alemania

dc.description.fil
Fil: Herrera, Maria Georgina. Universidad de Buenos Aires; Argentina. Ruhr Universität Bochum; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania
dc.journal.title
Biophysical Reviews
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s12551-021-00856-z
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