Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestion

Autores
Sabbione, Ana Clara; Nardo, Agustina Estefanía; Añón, María Cristina; Scilingo, Adriana Alicia
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Amaranth protein isolate was obtained and subjected to simulated gastrointestinal digestion to evaluate its potential antithrombotic activity. The protein isolate did not present fibrin clotting inhibition at the concentrations studied, whereas the hydrolysate (DH% = 51.1 ± 3.8%) exhibited inhibition of fibrin coagulation, showing a dose–response behaviour (IC50 = 0.23 ± 0.02 mg/mL), confirming that the enzymatic treatment was able to release bioactive peptides from amaranth proteins. A fraction with high antithrombotic activity was obtained from this hydrolysate, and resulted to be three times more potent than its original sample (IC50 = 0.07 ± 0.01 mg/mL). The absorption of this active fraction was studied with an in vitro peptides transport assay through intestinal epithelium and it was observed that some peptides are able to cross the Caco2-TC7 cell monolayer. Potentially bioactive peptides were found after sequencing them, and informatics tools allowed us to select and locate in their native molecules those peptides prone to inhibit thrombin activity.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
Materia
Ciencias Exactas
Amaranth protein isolate
Gastrointestinal digestion
Antithrombotic activity
Absorption by Caco 2 cell culture
Bioactive peptides
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:10915/108335
Acceder
id SEDICI_a8ed6e478cd3de2ed82896e20dd4f93b
oai_identifier_str oai:sedici.unlp.edu.ar:10915/108335
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestionSabbione, Ana ClaraNardo, Agustina EstefaníaAñón, María CristinaScilingo, Adriana AliciaCiencias ExactasAmaranth protein isolateGastrointestinal digestionAntithrombotic activityAbsorption by Caco 2 cell cultureBioactive peptidesAmaranth protein isolate was obtained and subjected to simulated gastrointestinal digestion to evaluate its potential antithrombotic activity. The protein isolate did not present fibrin clotting inhibition at the concentrations studied, whereas the hydrolysate (DH% = 51.1 ± 3.8%) exhibited inhibition of fibrin coagulation, showing a dose–response behaviour (IC<i>50</i> = 0.23 ± 0.02 mg/mL), confirming that the enzymatic treatment was able to release bioactive peptides from amaranth proteins. A fraction with high antithrombotic activity was obtained from this hydrolysate, and resulted to be three times more potent than its original sample (IC<i>50</i> = 0.07 ± 0.01 mg/mL). The absorption of this active fraction was studied with an in vitro peptides transport assay through intestinal epithelium and it was observed that some peptides are able to cross the Caco2-TC7 cell monolayer. Potentially bioactive peptides were found after sequencing them, and informatics tools allowed us to select and locate in their native molecules those peptides prone to inhibit thrombin activity.Centro de Investigación y Desarrollo en Criotecnología de Alimentos2015-11-21info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf204-214http://sedici.unlp.edu.ar/handle/10915/108335enginfo:eu-repo/semantics/altIdentifier/issn/1756-4646info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jff.2015.10.015info: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:UNLP2025-09-10T12:27:12Zoai:sedici.unlp.edu.ar:10915/108335Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-10 12:27:12.861SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestion
title Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestion
spellingShingle Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestion
Sabbione, Ana Clara
Ciencias Exactas
Amaranth protein isolate
Gastrointestinal digestion
Antithrombotic activity
Absorption by Caco 2 cell culture
Bioactive peptides
title_short Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestion
title_full Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestion
title_fullStr Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestion
title_full_unstemmed Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestion
title_sort Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestion
dc.creator.none.fl_str_mv Sabbione, Ana Clara
Nardo, Agustina Estefanía
Añón, María Cristina
Scilingo, Adriana Alicia
author Sabbione, Ana Clara
author_facet Sabbione, Ana Clara
Nardo, Agustina Estefanía
Añón, María Cristina
Scilingo, Adriana Alicia
author_role author
author2 Nardo, Agustina Estefanía
Añón, María Cristina
Scilingo, Adriana Alicia
author2_role author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Amaranth protein isolate
Gastrointestinal digestion
Antithrombotic activity
Absorption by Caco 2 cell culture
Bioactive peptides
topic Ciencias Exactas
Amaranth protein isolate
Gastrointestinal digestion
Antithrombotic activity
Absorption by Caco 2 cell culture
Bioactive peptides
dc.description.none.fl_txt_mv Amaranth protein isolate was obtained and subjected to simulated gastrointestinal digestion to evaluate its potential antithrombotic activity. The protein isolate did not present fibrin clotting inhibition at the concentrations studied, whereas the hydrolysate (DH% = 51.1 ± 3.8%) exhibited inhibition of fibrin coagulation, showing a dose–response behaviour (IC<i>50</i> = 0.23 ± 0.02 mg/mL), confirming that the enzymatic treatment was able to release bioactive peptides from amaranth proteins. A fraction with high antithrombotic activity was obtained from this hydrolysate, and resulted to be three times more potent than its original sample (IC<i>50</i> = 0.07 ± 0.01 mg/mL). The absorption of this active fraction was studied with an in vitro peptides transport assay through intestinal epithelium and it was observed that some peptides are able to cross the Caco2-TC7 cell monolayer. Potentially bioactive peptides were found after sequencing them, and informatics tools allowed us to select and locate in their native molecules those peptides prone to inhibit thrombin activity.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
description Amaranth protein isolate was obtained and subjected to simulated gastrointestinal digestion to evaluate its potential antithrombotic activity. The protein isolate did not present fibrin clotting inhibition at the concentrations studied, whereas the hydrolysate (DH% = 51.1 ± 3.8%) exhibited inhibition of fibrin coagulation, showing a dose–response behaviour (IC<i>50</i> = 0.23 ± 0.02 mg/mL), confirming that the enzymatic treatment was able to release bioactive peptides from amaranth proteins. A fraction with high antithrombotic activity was obtained from this hydrolysate, and resulted to be three times more potent than its original sample (IC<i>50</i> = 0.07 ± 0.01 mg/mL). The absorption of this active fraction was studied with an in vitro peptides transport assay through intestinal epithelium and it was observed that some peptides are able to cross the Caco2-TC7 cell monolayer. Potentially bioactive peptides were found after sequencing them, and informatics tools allowed us to select and locate in their native molecules those peptides prone to inhibit thrombin activity.
publishDate 2015
dc.date.none.fl_str_mv 2015-11-21
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/10915/108335
url http://sedici.unlp.edu.ar/handle/10915/108335
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.2015.10.015
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
204-214
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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score 12.885934

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