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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  
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OLIGOMERS  
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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