Journal
FOODS
Volume 6, Issue 12, Pages -Publisher
MDPI
DOI: 10.3390/foods6120108
Keywords
oats; Avena sativa; bioactive peptides; ACE-I; renin; DPP-IV; renin-angiotensin-aldosterone system
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Funding
- Irish Department of Agriculture, Food and Marine (DAFM) [FIRM 11/SF/317]
- Spanish Ministry of Economy, Industry, and Competitiveness [FJCI-2016-29541]
- [2016073]
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The 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.
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