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...
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2021
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oai:doaj.org-article:44a16b8ee11e429d9e06c4d5c2357f7e2021-11-30T04:17:46ZPeptides derived from the gastrointestinal digestion of amaranth 11S globulin: Structure and antioxidant functionality2666-566210.1016/j.fochms.2021.100053https://doaj.org/article/44a16b8ee11e429d9e06c4d5c2357f7e2021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2666566221000447https://doaj.org/toc/2666-5662The 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/H2O2-induced-LDL oxidation. In a cellular system (H2O2-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.Susan García FilleríaAgustina Estefania NardoMargot PaulinoValeria TironiElsevierarticleAmaranth peptidesAntioxidant activityPhysico-chemical propertiesStructuresGastrointestinal digestionNutrition. Foods and food supplyTX341-641ENFood Chemistry: Molecular Sciences, Vol 3, Iss , Pp 100053- (2021) |
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Amaranth peptides Antioxidant activity Physico-chemical properties Structures Gastrointestinal digestion Nutrition. Foods and food supply TX341-641 |
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Amaranth peptides Antioxidant activity Physico-chemical properties Structures Gastrointestinal digestion Nutrition. Foods and food supply TX341-641 Susan García Fillería Agustina Estefania Nardo Margot Paulino Valeria Tironi Peptides derived from the gastrointestinal digestion of amaranth 11S globulin: Structure and antioxidant functionality |
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/H2O2-induced-LDL oxidation. In a cellular system (H2O2-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 |
article |
author |
Susan García Fillería Agustina Estefania Nardo Margot Paulino Valeria Tironi |
author_facet |
Susan García Fillería Agustina Estefania Nardo Margot Paulino Valeria Tironi |
author_sort |
Susan García Fillería |
title |
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_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_sort |
peptides derived from the gastrointestinal digestion of amaranth 11s globulin: structure and antioxidant functionality |
publisher |
Elsevier |
publishDate |
2021 |
url |
https://doaj.org/article/44a16b8ee11e429d9e06c4d5c2357f7e |
work_keys_str_mv |
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1718406740189380608 |