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Identification of New Peptides from Fermented Milk Showing Antioxidant Properties: Mechanism of Action

Due to their beneficial properties, fermented foods are considered important constituents of the human diet. They also contain bioactive peptides, health-promoting compounds studied for a wide range of effects. In this work, several antioxidant peptides extracted from fermented milk proteins were in...

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Autores principales: Tonolo, Federica, Fiorese, Federico, Moretto, Laura, Folda, Alessandra, Scalcon, Valeria, Grinzato, Alessandro, Ferro, Stefania, Arrigoni, Giorgio, Bindoli, Alberto, Feller, Emiliano, Bellamio, Marco, Marin, Oriano, Rigobello, Maria Pia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7070694/
https://www.ncbi.nlm.nih.gov/pubmed/32013158
http://dx.doi.org/10.3390/antiox9020117
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author Tonolo, Federica
Fiorese, Federico
Moretto, Laura
Folda, Alessandra
Scalcon, Valeria
Grinzato, Alessandro
Ferro, Stefania
Arrigoni, Giorgio
Bindoli, Alberto
Feller, Emiliano
Bellamio, Marco
Marin, Oriano
Rigobello, Maria Pia
author_facet Tonolo, Federica
Fiorese, Federico
Moretto, Laura
Folda, Alessandra
Scalcon, Valeria
Grinzato, Alessandro
Ferro, Stefania
Arrigoni, Giorgio
Bindoli, Alberto
Feller, Emiliano
Bellamio, Marco
Marin, Oriano
Rigobello, Maria Pia
author_sort Tonolo, Federica
collection PubMed
description Due to their beneficial properties, fermented foods are considered important constituents of the human diet. They also contain bioactive peptides, health-promoting compounds studied for a wide range of effects. In this work, several antioxidant peptides extracted from fermented milk proteins were investigated. First, enriched peptide fractions were purified and analysed for their antioxidant capacity in vitro and in a cellular model. Subsequently, from the most active fractions, 23 peptides were identified by mass spectrometry MS/MS), synthesized and tested. Peptides N-15-M, E-11-F, Q-14-R and A-17-E were selected for their antioxidant effects on Caco-2 cells both in the protection against oxidative stress and inhibition of ROS production. To define their action mechanism, the activation of the Kelch-like ECH-associated protein 1/nuclear factor erythroid 2-related factor 2(Keap1/Nrf2) pathway was studied evaluating the translocation of Nrf2 from cytosol to nucleus. In cells treated with N-15-M, Q-14-R and A-17-E, a higher amount of Nrf2 was found in the nucleus with respect to the control. In addition, the three active peptides, through the activation of Keap1/Nrf2 pathway, led to overexpression and increased activity of antioxidant enzymes. Molecular docking analysis confirmed the potential ability of N-15-M, Q-14-R and A-17-E to bind Keap1, showing their destabilizing effect on Keap1/Nrf2 interaction.
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spelling pubmed-70706942020-03-19 Identification of New Peptides from Fermented Milk Showing Antioxidant Properties: Mechanism of Action Tonolo, Federica Fiorese, Federico Moretto, Laura Folda, Alessandra Scalcon, Valeria Grinzato, Alessandro Ferro, Stefania Arrigoni, Giorgio Bindoli, Alberto Feller, Emiliano Bellamio, Marco Marin, Oriano Rigobello, Maria Pia Antioxidants (Basel) Article Due to their beneficial properties, fermented foods are considered important constituents of the human diet. They also contain bioactive peptides, health-promoting compounds studied for a wide range of effects. In this work, several antioxidant peptides extracted from fermented milk proteins were investigated. First, enriched peptide fractions were purified and analysed for their antioxidant capacity in vitro and in a cellular model. Subsequently, from the most active fractions, 23 peptides were identified by mass spectrometry MS/MS), synthesized and tested. Peptides N-15-M, E-11-F, Q-14-R and A-17-E were selected for their antioxidant effects on Caco-2 cells both in the protection against oxidative stress and inhibition of ROS production. To define their action mechanism, the activation of the Kelch-like ECH-associated protein 1/nuclear factor erythroid 2-related factor 2(Keap1/Nrf2) pathway was studied evaluating the translocation of Nrf2 from cytosol to nucleus. In cells treated with N-15-M, Q-14-R and A-17-E, a higher amount of Nrf2 was found in the nucleus with respect to the control. In addition, the three active peptides, through the activation of Keap1/Nrf2 pathway, led to overexpression and increased activity of antioxidant enzymes. Molecular docking analysis confirmed the potential ability of N-15-M, Q-14-R and A-17-E to bind Keap1, showing their destabilizing effect on Keap1/Nrf2 interaction. MDPI 2020-01-29 /pmc/articles/PMC7070694/ /pubmed/32013158 http://dx.doi.org/10.3390/antiox9020117 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Tonolo, Federica
Fiorese, Federico
Moretto, Laura
Folda, Alessandra
Scalcon, Valeria
Grinzato, Alessandro
Ferro, Stefania
Arrigoni, Giorgio
Bindoli, Alberto
Feller, Emiliano
Bellamio, Marco
Marin, Oriano
Rigobello, Maria Pia
Identification of New Peptides from Fermented Milk Showing Antioxidant Properties: Mechanism of Action
title Identification of New Peptides from Fermented Milk Showing Antioxidant Properties: Mechanism of Action
title_full Identification of New Peptides from Fermented Milk Showing Antioxidant Properties: Mechanism of Action
title_fullStr Identification of New Peptides from Fermented Milk Showing Antioxidant Properties: Mechanism of Action
title_full_unstemmed Identification of New Peptides from Fermented Milk Showing Antioxidant Properties: Mechanism of Action
title_short Identification of New Peptides from Fermented Milk Showing Antioxidant Properties: Mechanism of Action
title_sort identification of new peptides from fermented milk showing antioxidant properties: mechanism of action
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7070694/
https://www.ncbi.nlm.nih.gov/pubmed/32013158
http://dx.doi.org/10.3390/antiox9020117
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