Peptides of amaranth were targeted as containing sequences with potential anti-inflammatory properties

Autores
Moronta, Julián; Smaldini, Paola Lorena; Docena, Guillermo Horacio; Añón, María Cristina
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The immunomodulatory effect of amaranth peptides on epithelial cells activated through the NF-κB signalling pathway was examined. Results showed that extensive protein hydrolysis from amaranth (23 and 30% degree of hydrolysis) reduced the emission of light in bacterial flagellin-activated Caco-2 CCL20: luc cells (Caco-2 cells transfected with a luciferase reporter under the control of the CCL20 promoter) compared with the non-hydrolysed protein. Purification of the most active peptide fractions by HPLC chromatography and sequencing showed that the peptide SSEDIKE possessed a modulatory capacity on activated cells to suppress the expression of mRNA coding for CCL20. This peptide was non-toxic for cells. These findings indicated that the peptide SSEDIKE derived from proteins of amaranth attenuated the activation of human intestinal epithelial cell, and hence amaranth proteins could be included in functional foods as a source of bioactive peptides with health promoting properties.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
Materia
Ciencias Exactas
Amaranth peptides
Immunomodulatory activity
Anti-inflammatory
Intestinal epithelial cells
CCL20
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/108244

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repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Peptides of amaranth were targeted as containing sequences with potential anti-inflammatory propertiesMoronta, JuliánSmaldini, Paola LorenaDocena, Guillermo HoracioAñón, María CristinaCiencias ExactasAmaranth peptidesImmunomodulatory activityAnti-inflammatoryIntestinal epithelial cellsCCL20The immunomodulatory effect of amaranth peptides on epithelial cells activated through the NF-κB signalling pathway was examined. Results showed that extensive protein hydrolysis from amaranth (23 and 30% degree of hydrolysis) reduced the emission of light in bacterial flagellin-activated Caco-2 CCL20: luc cells (Caco-2 cells transfected with a luciferase reporter under the control of the CCL20 promoter) compared with the non-hydrolysed protein. Purification of the most active peptide fractions by HPLC chromatography and sequencing showed that the peptide SSEDIKE possessed a modulatory capacity on activated cells to suppress the expression of mRNA coding for CCL20. This peptide was non-toxic for cells. These findings indicated that the peptide SSEDIKE derived from proteins of amaranth attenuated the activation of human intestinal epithelial cell, and hence amaranth proteins could be included in functional foods as a source of bioactive peptides with health promoting properties.Centro de Investigación y Desarrollo en Criotecnología de Alimentos2016info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf463-473http://sedici.unlp.edu.ar/handle/10915/108244enginfo:eu-repo/semantics/altIdentifier/issn/1756-4646info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jff.2015.12.022info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-15T11:16:26Zoai:sedici.unlp.edu.ar:10915/108244Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-15 11:16:26.527SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Peptides of amaranth were targeted as containing sequences with potential anti-inflammatory properties
title Peptides of amaranth were targeted as containing sequences with potential anti-inflammatory properties
spellingShingle Peptides of amaranth were targeted as containing sequences with potential anti-inflammatory properties
Moronta, Julián
Ciencias Exactas
Amaranth peptides
Immunomodulatory activity
Anti-inflammatory
Intestinal epithelial cells
CCL20
title_short Peptides of amaranth were targeted as containing sequences with potential anti-inflammatory properties
title_full Peptides of amaranth were targeted as containing sequences with potential anti-inflammatory properties
title_fullStr Peptides of amaranth were targeted as containing sequences with potential anti-inflammatory properties
title_full_unstemmed Peptides of amaranth were targeted as containing sequences with potential anti-inflammatory properties
title_sort Peptides of amaranth were targeted as containing sequences with potential anti-inflammatory properties
dc.creator.none.fl_str_mv Moronta, Julián
Smaldini, Paola Lorena
Docena, Guillermo Horacio
Añón, María Cristina
author Moronta, Julián
author_facet Moronta, Julián
Smaldini, Paola Lorena
Docena, Guillermo Horacio
Añón, María Cristina
author_role author
author2 Smaldini, Paola Lorena
Docena, Guillermo Horacio
Añón, María Cristina
author2_role author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Amaranth peptides
Immunomodulatory activity
Anti-inflammatory
Intestinal epithelial cells
CCL20
topic Ciencias Exactas
Amaranth peptides
Immunomodulatory activity
Anti-inflammatory
Intestinal epithelial cells
CCL20
dc.description.none.fl_txt_mv The immunomodulatory effect of amaranth peptides on epithelial cells activated through the NF-κB signalling pathway was examined. Results showed that extensive protein hydrolysis from amaranth (23 and 30% degree of hydrolysis) reduced the emission of light in bacterial flagellin-activated Caco-2 CCL20: luc cells (Caco-2 cells transfected with a luciferase reporter under the control of the CCL20 promoter) compared with the non-hydrolysed protein. Purification of the most active peptide fractions by HPLC chromatography and sequencing showed that the peptide SSEDIKE possessed a modulatory capacity on activated cells to suppress the expression of mRNA coding for CCL20. This peptide was non-toxic for cells. These findings indicated that the peptide SSEDIKE derived from proteins of amaranth attenuated the activation of human intestinal epithelial cell, and hence amaranth proteins could be included in functional foods as a source of bioactive peptides with health promoting properties.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
description The immunomodulatory effect of amaranth peptides on epithelial cells activated through the NF-κB signalling pathway was examined. Results showed that extensive protein hydrolysis from amaranth (23 and 30% degree of hydrolysis) reduced the emission of light in bacterial flagellin-activated Caco-2 CCL20: luc cells (Caco-2 cells transfected with a luciferase reporter under the control of the CCL20 promoter) compared with the non-hydrolysed protein. Purification of the most active peptide fractions by HPLC chromatography and sequencing showed that the peptide SSEDIKE possessed a modulatory capacity on activated cells to suppress the expression of mRNA coding for CCL20. This peptide was non-toxic for cells. These findings indicated that the peptide SSEDIKE derived from proteins of amaranth attenuated the activation of human intestinal epithelial cell, and hence amaranth proteins could be included in functional foods as a source of bioactive peptides with health promoting properties.
publishDate 2016
dc.date.none.fl_str_mv 2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/108244
url http://sedici.unlp.edu.ar/handle/10915/108244
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1756-4646
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jff.2015.12.022
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
463-473
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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