Cargando…
Peptides derived from the gastrointestinal digestion of amaranth 11S globulin: Structure and antioxidant functionality
The relationship between structural and physicochemical properties and antioxidant activity of peptides from amaranth 11S-globulin was studied. Peptides AWEEREQGSR, TEVWDSNEQ, IYIEQGNGITGM and YLAGKPQQEH had the greatest in vitro activity (ORAC, HORAC). GDRFQDQHQ, HVIKPPSRA and KFNRPETT were the mos...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8991498/ https://www.ncbi.nlm.nih.gov/pubmed/35415655 http://dx.doi.org/10.1016/j.fochms.2021.100053 |
_version_ | 1784683580222341120 |
---|---|
author | Fillería, Susan García Nardo, Agustina Estefania Paulino, Margot Tironi, Valeria |
author_facet | Fillería, Susan García Nardo, Agustina Estefania Paulino, Margot Tironi, Valeria |
author_sort | Fillería, Susan García |
collection | PubMed |
description | The relationship between structural and physicochemical properties and antioxidant activity of peptides from amaranth 11S-globulin was studied. Peptides AWEEREQGSR, TEVWDSNEQ, IYIEQGNGITGM and YLAGKPQQEH had the greatest in vitro activity (ORAC, HORAC). GDRFQDQHQ, HVIKPPSRA and KFNRPETT were the most active ones against Cu(+2)/H(2)O(2)-induced-LDL oxidation. In a cellular system (H(2)O(2)-induced-Caco2-TC7), TEVWDSNEQ, IYIEQGNGITGM, GDRFQDQHQ, LAGKPQQEHSGEHQ and KFNRPETT were the most effective in decreasing ROS, while the effects on SOD, GPx, and GSH were variable. To understand the structure–antioxidant activity relationships, the content of aromatic and acidic amino acids, the degree of hydrophobicity and the charge distribution on the accessible surface of peptides structures obtained by molecular dynamics were analysed. The low correlation between in vitro, ex vivo and cellular activities could be explained by the influence of physicochemical and structural properties on the interaction with complex systems (LDL/cells), peptide modifications and/or mechanisms other than direct ROS inhibition in the cells. |
format | Online Article Text |
id | pubmed-8991498 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-89914982022-04-11 Peptides derived from the gastrointestinal digestion of amaranth 11S globulin: Structure and antioxidant functionality Fillería, Susan García Nardo, Agustina Estefania Paulino, Margot Tironi, Valeria Food Chem (Oxf) Article(s) from the Special Issue on Proteomic approaches in the identification of food proteins and peptides by Dr Toldrá and Dr. Mora The relationship between structural and physicochemical properties and antioxidant activity of peptides from amaranth 11S-globulin was studied. Peptides AWEEREQGSR, TEVWDSNEQ, IYIEQGNGITGM and YLAGKPQQEH had the greatest in vitro activity (ORAC, HORAC). GDRFQDQHQ, HVIKPPSRA and KFNRPETT were the most active ones against Cu(+2)/H(2)O(2)-induced-LDL oxidation. In a cellular system (H(2)O(2)-induced-Caco2-TC7), TEVWDSNEQ, IYIEQGNGITGM, GDRFQDQHQ, LAGKPQQEHSGEHQ and KFNRPETT were the most effective in decreasing ROS, while the effects on SOD, GPx, and GSH were variable. To understand the structure–antioxidant activity relationships, the content of aromatic and acidic amino acids, the degree of hydrophobicity and the charge distribution on the accessible surface of peptides structures obtained by molecular dynamics were analysed. The low correlation between in vitro, ex vivo and cellular activities could be explained by the influence of physicochemical and structural properties on the interaction with complex systems (LDL/cells), peptide modifications and/or mechanisms other than direct ROS inhibition in the cells. Elsevier 2021-11-18 /pmc/articles/PMC8991498/ /pubmed/35415655 http://dx.doi.org/10.1016/j.fochms.2021.100053 Text en © 2021 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article(s) from the Special Issue on Proteomic approaches in the identification of food proteins and peptides by Dr Toldrá and Dr. Mora Fillería, Susan García Nardo, Agustina Estefania Paulino, Margot Tironi, Valeria Peptides derived from the gastrointestinal digestion of amaranth 11S globulin: Structure and antioxidant functionality |
title | Peptides derived from the gastrointestinal digestion of amaranth 11S globulin: Structure and antioxidant functionality |
title_full | Peptides derived from the gastrointestinal digestion of amaranth 11S globulin: Structure and antioxidant functionality |
title_fullStr | Peptides derived from the gastrointestinal digestion of amaranth 11S globulin: Structure and antioxidant functionality |
title_full_unstemmed | Peptides derived from the gastrointestinal digestion of amaranth 11S globulin: Structure and antioxidant functionality |
title_short | Peptides derived from the gastrointestinal digestion of amaranth 11S globulin: Structure and antioxidant functionality |
title_sort | peptides derived from the gastrointestinal digestion of amaranth 11s globulin: structure and antioxidant functionality |
topic | Article(s) from the Special Issue on Proteomic approaches in the identification of food proteins and peptides by Dr Toldrá and Dr. Mora |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8991498/ https://www.ncbi.nlm.nih.gov/pubmed/35415655 http://dx.doi.org/10.1016/j.fochms.2021.100053 |
work_keys_str_mv | AT filleriasusangarcia peptidesderivedfromthegastrointestinaldigestionofamaranth11sglobulinstructureandantioxidantfunctionality AT nardoagustinaestefania peptidesderivedfromthegastrointestinaldigestionofamaranth11sglobulinstructureandantioxidantfunctionality AT paulinomargot peptidesderivedfromthegastrointestinaldigestionofamaranth11sglobulinstructureandantioxidantfunctionality AT tironivaleria peptidesderivedfromthegastrointestinaldigestionofamaranth11sglobulinstructureandantioxidantfunctionality |