Mechanisms of food protein-derived antihypertensive peptides other than ACE inhibition

Hypertension is an important risk factor for developing cardiovascular disease and a major contributor to global mortality. Cryptic bioactive peptides released from food proteins have been widely pursued for the management of hypertension, mostly based on their perceived activity in inhibiting angiotensin I-converting enzyme of the physiological blood pressure-regulating renin angiotensin system (RAS) pathway. However, there is considerable evidence that food protein-derived peptides can interact with other RAS steps and related pathways in the vascular system, potentially contributing to blood pressure reduction. This contribution highlights these plausible antihypertensive mechanisms induced by food peptides other than ACE inhibition including renin and endothelin system inhibition, angiotensin receptor and calcium channel blocking, and arginine-nitric oxide pathway-mediated effects. It appears that the antihypertensive peptides and hydrolysates may employ concerted mechanisms at the protein and gene levels in regulating elevated blood pressure during hypertension, suggesting the need for comprehensive characterization of their interaction with the cardiovascular system.