Insights into gliadin supramolecular organization at digestive pH 3.0

Autores
Herrera, Maria Georgina; Vazquez, Diego Sebastian; Sreij, R.; Drechsler, M.; Hertle, Y.; Hellweg, T.; Dodero, Veronica Isabel
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Herrera, Maria Georgina. Universitat Bielefeld; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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
Fil: Sreij, R.. Universitat Bielefeld; Alemania
Fil: Drechsler, M.. University of Bayreuth; Alemania
Fil: Hertle, Y.. Universitat Bielefeld; Alemania
Fil: Hellweg, T.. Universitat Bielefeld; Alemania
Fil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania
Materia
CELIAC DISEASE
GLIADIN
GLUTEN-RELATED DISORDERS
MOLECULAR SIMULATION
OLIGOMERS
SAXS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/93102
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/93102
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Insights into gliadin supramolecular organization at digestive pH 3.0Herrera, Maria GeorginaVazquez, Diego SebastianSreij, R.Drechsler, M.Hertle, Y.Hellweg, T.Dodero, Veronica IsabelCELIAC DISEASEGLIADINGLUTEN-RELATED DISORDERSMOLECULAR SIMULATIONOLIGOMERSSAXShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Alpha-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.Fil: Herrera, Maria Georgina. Universitat Bielefeld; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: 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; ArgentinaFil: Sreij, R.. Universitat Bielefeld; AlemaniaFil: Drechsler, M.. University of Bayreuth; AlemaniaFil: Hertle, Y.. Universitat Bielefeld; AlemaniaFil: Hellweg, T.. Universitat Bielefeld; AlemaniaFil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; AlemaniaElsevier Science2018-05-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/93102Herrera, 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; 363-3700927-7765CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://linkinghub.elsevier.com/retrieve/pii/S0927776518301280info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2018.02.053info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-29T11:48:53Zoai:ri.conicet.gov.ar:11336/93102instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-29 11:48:54.075CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Insights into gliadin supramolecular organization at digestive pH 3.0
title Insights into gliadin supramolecular organization at digestive pH 3.0
spellingShingle Insights into gliadin supramolecular organization at digestive pH 3.0
Herrera, Maria Georgina
CELIAC DISEASE
GLIADIN
GLUTEN-RELATED DISORDERS
MOLECULAR SIMULATION
OLIGOMERS
SAXS
title_short Insights into gliadin supramolecular organization at digestive pH 3.0
title_full Insights into gliadin supramolecular organization at digestive pH 3.0
title_fullStr Insights into gliadin supramolecular organization at digestive pH 3.0
title_full_unstemmed Insights into gliadin supramolecular organization at digestive pH 3.0
title_sort Insights into gliadin supramolecular organization at digestive pH 3.0
dc.creator.none.fl_str_mv Herrera, Maria Georgina
Vazquez, Diego Sebastian
Sreij, R.
Drechsler, M.
Hertle, Y.
Hellweg, T.
Dodero, Veronica Isabel
author Herrera, Maria Georgina
author_facet Herrera, Maria Georgina
Vazquez, Diego Sebastian
Sreij, R.
Drechsler, M.
Hertle, Y.
Hellweg, T.
Dodero, Veronica Isabel
author_role author
author2 Vazquez, Diego Sebastian
Sreij, R.
Drechsler, M.
Hertle, Y.
Hellweg, T.
Dodero, Veronica Isabel
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv CELIAC DISEASE
GLIADIN
GLUTEN-RELATED DISORDERS
MOLECULAR SIMULATION
OLIGOMERS
SAXS
topic CELIAC DISEASE
GLIADIN
GLUTEN-RELATED DISORDERS
MOLECULAR SIMULATION
OLIGOMERS
SAXS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
Fil: Herrera, Maria Georgina. Universitat Bielefeld; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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
Fil: Sreij, R.. Universitat Bielefeld; Alemania
Fil: Drechsler, M.. University of Bayreuth; Alemania
Fil: Hertle, Y.. Universitat Bielefeld; Alemania
Fil: Hellweg, T.. Universitat Bielefeld; Alemania
Fil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania
description 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.
publishDate 2018
dc.date.none.fl_str_mv 2018-05-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/93102
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
0927-7765
CONICET Digital
CONICET
url http://hdl.handle.net/11336/93102
identifier_str_mv 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
0927-7765
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://linkinghub.elsevier.com/retrieve/pii/S0927776518301280
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2018.02.053
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.10058

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