{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Martineau-Cote D"],"funding":["Pulse Science Research Cluster 3-Activity ASC-06 Activity 14A"],"pagination":["6432-6443"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10979453"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["72(12)"],"pubmed_abstract":["Faba bean flour, after <i>in vitro</i> gastrointestinal digestion, showed important antioxidant and angiotensin-converting enzyme (ACE) inhibitory activities. In the present study, 11 faba bean- derived peptides were synthesized to confirm their bioactivities and provide a deeper understanding of their mechanisms of action. The results revealed that 7 peptides were potent antioxidants, namely, NYDEGSEPR, TETWNPNHPEL, TETWNPNHPE, VIPTEPPH, VIPTEPPHA, VVIPTEPPHA, and VVIPTEPPH. Among them, TETWNPNHPEL had the highest activity in the ABTS (EC<sub>50</sub> = 0.5 ± 0.2 mM) and DPPH (EC<sub>50</sub> = 2.1 ± 0.1 mM) assays (<i>p</i> < 0.05), whereas TETWNPNHPE had the highest activity (<i>p</i> < 0.05) in the ORAC assay (2.84 ± 0.08 mM Trolox equivalent/mM). Synergistic and/or additive effects were found when selected peptides (TETWNPNHPEL, NYDEGSEPR, and VVIPTEPPHA) were combined. Four peptides were potent ACE inhibitors, where VVIPTEPPH (IC<sub>50</sub> = 43 ± 1 μM) and VVIPTEPPHA (IC<sub>50</sub> = 50 ± 5 μM) had the highest activity (<i>p</i> < 0.05), followed by VIPTEPPH (IC<sub>50</sub> = 90 ± 10 μM) and then VIPTEPPHA (IC<sub>50</sub> = 123 ± 5 μM) (<i>p</i> < 0.05). These peptides were noncompetitive inhibitors, as supported by kinetic studies and a molecular docking investigation. This study demonstrated that peptides derived from faba beans have multifunctional bioactivities, making them a promising food-functional and nutraceutical ingredient."],"journal":["Journal of agricultural and food chemistry"],"pubmed_title":["Antioxidant and Angiotensin-Converting Enzyme Inhibitory Activity of Faba Bean-Derived Peptides After <i>In Vitro</i> Gastrointestinal Digestion: Insight into Their Mechanism of Action."],"pmcid":["PMC10979453"],"funding_grant_id":["J-001964"],"pubmed_authors":["L'Hocine L","Martineau-Cote D","Achouri A","Karboune S"],"additional_accession":[]},"is_claimable":false,"name":"Antioxidant and Angiotensin-Converting Enzyme Inhibitory Activity of Faba Bean-Derived Peptides After <i>In Vitro</i> Gastrointestinal Digestion: Insight into Their Mechanism of Action.","description":"Faba bean flour, after <i>in vitro</i> gastrointestinal digestion, showed important antioxidant and angiotensin-converting enzyme (ACE) inhibitory activities. In the present study, 11 faba bean- derived peptides were synthesized to confirm their bioactivities and provide a deeper understanding of their mechanisms of action. The results revealed that 7 peptides were potent antioxidants, namely, NYDEGSEPR, TETWNPNHPEL, TETWNPNHPE, VIPTEPPH, VIPTEPPHA, VVIPTEPPHA, and VVIPTEPPH. Among them, TETWNPNHPEL had the highest activity in the ABTS (EC<sub>50</sub> = 0.5 ± 0.2 mM) and DPPH (EC<sub>50</sub> = 2.1 ± 0.1 mM) assays (<i>p</i> < 0.05), whereas TETWNPNHPE had the highest activity (<i>p</i> < 0.05) in the ORAC assay (2.84 ± 0.08 mM Trolox equivalent/mM). Synergistic and/or additive effects were found when selected peptides (TETWNPNHPEL, NYDEGSEPR, and VVIPTEPPHA) were combined. Four peptides were potent ACE inhibitors, where VVIPTEPPH (IC<sub>50</sub> = 43 ± 1 μM) and VVIPTEPPHA (IC<sub>50</sub> = 50 ± 5 μM) had the highest activity (<i>p</i> < 0.05), followed by VIPTEPPH (IC<sub>50</sub> = 90 ± 10 μM) and then VIPTEPPHA (IC<sub>50</sub> = 123 ± 5 μM) (<i>p</i> < 0.05). These peptides were noncompetitive inhibitors, as supported by kinetic studies and a molecular docking investigation. This study demonstrated that peptides derived from faba beans have multifunctional bioactivities, making them a promising food-functional and nutraceutical ingredient.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2025-04-21T21:27:40.356Z","creation":"2025-04-05T18:25:33.929Z"},"accession":"S-EPMC10979453","cross_references":{"pubmed":["38470110"],"doi":["10.1021/acs.jafc.4c00829"]}}