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dc.contributor.author
Herrera, Maria Georgina
dc.contributor.author
Vazquez, Diego Sebastian
dc.contributor.author
Sreij, R.
dc.contributor.author
Drechsler, M.
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Hertle, Y.
dc.contributor.author
Hellweg, T.
dc.contributor.author
Dodero, Veronica Isabel
dc.date.available
2019-12-27T17:18:52Z
dc.date.issued
2018-05-01
dc.identifier.citation
Herrera, Maria Georgina; Vazquez, Diego Sebastian; Sreij, R.; Drechsler, M.; Hertle, Y.; et al.; Insights into gliadin supramolecular organization at digestive pH 3.0; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 165; 1-5-2018; 363-370
dc.identifier.issn
0927-7765
dc.identifier.uri
http://hdl.handle.net/11336/93102
dc.description.abstract
Alpha-gliadin is a highly immunogenic protein from wheat, which is associated with many human diseases, like celiac disease and non-celiac gluten sensitivity. Because of that, gliadin solution is subject to intense biomedical research. However, the physicochemical nature of the employed gliadin solution at physiological pH is not understood. Herein, we present a supramolecular evaluation of the alpha-gliadin protein in water at pH 3.0 by dynamic light scattering (DLS), cryo-transmission electron microscopy (cryo-TEM) and small-angle-.X-ray scattering (SAXS). We report that at 0.5 wt% concentration (0.1 mg/ml), gliadin is already a colloidal polydisperse system with an average hydrodynamic radius of 30 ± 10 nm. By cryo-TEM, we detected mainly large clusters. However, it was possible to visualise for the first time prolate oligomers of around 68 nm and 103 nm, minor and major axis, respectively. SAXS experiments support the existence of prolate/rod-like structures. At 1.5 wt% concentration gliadin dimers, small oligomers and large clusters coexist. The radius of gyration (Rg1) of gliadin dimer is 5.72 ± 0.23 nm with a dimer cross-section (Rc) of 1.63 nm, and an average length of around 19 nm, this suggests that gliadin dimers are formed longitudinally. Finally, our alpha-gliadin 3D model, obtained by ab initio prediction and analysed by molecular dynamics (MD), predicts that two surfaces prone to aggregation are exposed to the solvent, at the C-terminus. We hypothesise that this region may be involved in the dimerisation process of alpha-gliadin.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
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
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GLUTEN-RELATED DISORDERS
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MOLECULAR SIMULATION
dc.subject
OLIGOMERS
dc.subject
SAXS
dc.subject.classification
Biofísica
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Insights into gliadin supramolecular organization at digestive pH 3.0
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-21T19:01:08Z
dc.journal.volume
165
dc.journal.pagination
363-370
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Herrera, Maria Georgina. Universitat Bielefeld; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Vazquez, Diego Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
dc.description.fil
Fil: Sreij, R.. Universitat Bielefeld; Alemania
dc.description.fil
Fil: Drechsler, M.. University of Bayreuth; Alemania
dc.description.fil
Fil: Hertle, Y.. Universitat Bielefeld; Alemania
dc.description.fil
Fil: Hellweg, T.. Universitat Bielefeld; Alemania
dc.description.fil
Fil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania
dc.journal.title
Colloids and Surfaces B: Biointerfaces
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://linkinghub.elsevier.com/retrieve/pii/S0927776518301280
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.colsurfb.2018.02.053
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