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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/93102
Ver los metadatos del registro completo
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oai:ri.conicet.gov.ar:11336/93102 |
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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 Técnicas2025-09-29T09:49:36Zoai: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:34982025-09-29 09:49:37.121CONICET 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) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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13.070432 |