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dc.contributor.authorBleakley, Stephen
dc.contributor.authorHayes, Maria
dc.contributor.authorO’ Shea, Nora
dc.contributor.authorGallagher, Eimear
dc.contributor.authorLafarga, Tomas
dc.date.accessioned2024-02-24T17:11:42Z
dc.date.available2024-02-24T17:11:42Z
dc.date.issued2017-12-04
dc.identifier.citationBleakley, S.; Hayes, M.; O’ Shea, N.; Gallagher, E.; Lafarga, T. Predicted Release and Analysis of Novel ACE-I, Renin, and DPP-IV Inhibitory Peptides from Common Oat (Avena sativa) Protein Hydrolysates Using in Silico Analysis. Foods 2017, 6, 108. https://doi.org/10.3390/foods6120108en_US
dc.identifier.urihttp://hdl.handle.net/11019/3666
dc.descriptionpeer-revieweden_US
dc.description.abstractThe renin-angiotensin-aldosterone system (RAAS) plays an important role in regulating hypertension by controlling vasoconstriction and intravascular fluid volume. RAAS itself is largely regulated by the actions of renin (EC 3.4.23.15) and the angiotensin-I-converting enzyme (ACE-I; EC 3.4.15.1). The enzyme dipeptidyl peptidase-IV (DPP-IV; EC 3.4.14.5) also plays a role in the development of type-2 diabetes. The inhibition of the renin, ACE-I, and DPP-IV enzymes has therefore become a key therapeutic target for the treatment of hypertension and diabetes. The aim of this study was to assess the bioactivity of different oat (Avena sativa) protein isolates and their ability to inhibit the renin, ACE-I, and DPP-IV enzymes. In silico analysis was carried out to predictthe likelihood of bioactive inhibitory peptides occurring from oat protein hydrolysates following in silico hydrolysis with the proteases papain and ficin. Nine peptides, including FFG, IFFFL, PFL, WWK, WCY, FPIL, CPA, FLLA, and FEPL were subsequently chemically synthesised, and their bioactivities were confirmed using in vitro bioassays. The isolated oat proteins derived from seven different oat varieties were found to inhibit the ACE-I enzyme by between 86.5 ± 10.7% and 96.5 ± 25.8%, renin by between 40.5 ± 21.5% and 70.9 ± 7.6%, and DPP-IV by between 3.7 ± 3.9% and 46.2 ± 28.8%. The activity of the synthesised peptides was also determined.en_US
dc.language.isoenen_US
dc.publisherMultidisciplinary Digital Publishing Instituteen_US
dc.relation.ispartofseriesFoods;Vol 6
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectoatsen_US
dc.subjectAvena sativaen_US
dc.subjectbioactive peptidesen_US
dc.subjectACE-Ien_US
dc.subjectreninen_US
dc.subjectDPP-IVen_US
dc.subjectrenin-angiotensin-aldosterone systemen_US
dc.titlePredicted Release and Analysis of Novel ACE-I, Renin, and DPP-IV Inhibitory Peptides from Common Oat (Avena sativa) Protein Hydrolysates Using in Silico Analysisen_US
dc.typeArticleen_US
dc.identifier.doihttps://doi.org/10.3390/foods6120108
dc.contributor.sponsorTeagasc Walsh Fellowshipen_US
dc.contributor.sponsorIrish Department of Agriculture, Food and Marine (DAFM)en_US
dc.contributor.sponsorSpanish Ministry of Economy, Industry, and Competitivenessen_US
dc.contributor.sponsorGrantNumber2016073en_US
dc.contributor.sponsorGrantNumberFIRM 11/SF/317en_US
dc.contributor.sponsorGrantNumberFJCI-2016-29541en_US
dc.source.volume6
dc.source.issue12
dc.source.beginpage108
refterms.dateFOA2024-02-24T17:11:44Z
dc.source.journaltitleFoods


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