Modulation of Angiotensin-I-Converting Enzyme by Bioactive Peptides from Vegetable Origin

Bioactive peptides are small amino acid sequences that are inactive within a native protein. Its structures are formed by 2 or 20 amino acid residues. These biomolecules can regulate physiological processes and act as hormones or neurotransmitters. In recent years, bioactive peptides have been the subject of research because they can provide a benefit to human health. Peptides with antihypertensive activity have been the most studied because they can inhibit the activity of the angiotensin-converting enzyme (ACE-I), an enzyme related to blood pressure regulation by modulating the renin-angiotensin system (RAS). This characteristic has led to consider them a non-pharmacological alternative in the prevention and control of hypertension. The ACE-I is a metallopeptidase that has the function of converting the angiotensin-I decapeptide (DRVYIHPFHL) into the angiotensin-II octapeptide (DRVYIHHP) whose role is to produce a vasoconstrictor effect. Peptides with ACE-I inhibitory activity can inactivate the active site of this enzyme, these must have an aromatic or branched amino acid residues in the last three positions of the Cterminal region. However, the peptides can have different conformations, so that not only the amino acid sequence but their structure determines their inhibitory capacity. According to the above, peptides with ACE-I inhibitory activity could be incorporated into the elaboration of functional foods to be used as alternatives in the treatment of hypertension, once their biological effect has been demonstrated in vitro and in vivo.