title: Antihypertensive peptides from food proteins.
abstract: Bioactive peptides are encrypted within the primary structure of food proteins where they remain inactive until released by enzymatic hydrolysis. Once released from the parent protein, certain peptides have the ability to modulate the renin-angiotensin system (RAS) because they decrease activities of renin or angiotensin-converting enzyme (ACE), the two main enzymes that regulate mammalian blood pressure. These antihypertensive peptides can also enhance the endothelial nitric oxide synthase (eNOS) pathway to increase nitric oxide (NO) levels within vascular walls and promote vasodilation. The peptides can block the interactions between angiotensin II (vasoconstrictor) and angiotensin receptors, which can contribute to reduced blood pressure. This review focuses on the methods that are involved in antihypertensive peptide production from food sources, including fractionation protocols that are used to enrich bioactive peptide content and enhance peptide activity. It also discusses mechanisms that are believed to be involved in the antihypertensive activity of these peptides.
authors.affiliation: Department of Human Nutritional Sciences, University of Manitoba, Winnipeg, Manitoba, Canada R3T 2N2; email: rotimi.aluko@umanitoba.ca.
authors.forename: Rotimi E
authors.initials: RE
authors.lastname: Aluko
mesh_terms: D000959:Antihypertensive Agents / Q000494:pharmacology*; D005502:Food; D010455:Peptides / Q000494:pharmacology*; D011506:Proteins / Q000737:chemistry*
chemical_list: D000959:Antihypertensive Agents; D010455:Peptides; D011506:Proteins
keywords: angiotensin-converting enzyme; antihypertensive peptides; food proteins; protein hydrolysates; renin; spontaneously hypertensive rats