Purification and hypotensive activity of rapeseed protein-derived renin and angiotensin converting enzyme inhibitory peptides

A database consisting of 168 dipeptides and 140 tripeptides was constructed from published literature to study the quantitative structure--activity relationships of angiotensin I-converting enzyme (ACE) inhibitory peptides. Two models were computed using partial least squares regression based on the three z-scores of 20 coded amino acids and further validated by cross-validation and permutation tests. The two-component model could explain 73.2% of the Y-variance (inhibitor concentration that reduced enzyme activity by 50%, IC50) with the predictive ability of 71.1% for dipeptides, while the single-component model could explain 47.1% of the Y-variance with the predictive ability of 43.3% for tripeptides. Amino acid residues with bulky side chains as well as hydrophobic side chains were preferred for dipeptides. For tripeptides, the most favorable residues for the carboxyl terminus were aromatic amino acids, while positively charged amino acids were preferred for the middle position, and hydrophobic amino acids were preferred for the amino terminus. According to the models, the IC50 values of seven new peptides with matchable primary sequences within pea protein, bovine milk protein, and soybean were predicted. The predicted peptides were synthesized, and their IC50 values were validated through laboratory determination of inhibition of ACE activity.

High blood pressure is considered as a significant health problem worldwide. In addition to numerous preventive and therapeutic drug treatments, important advances have been achieved in the identification of dietary compounds that may contribute to cardiovascular health. Among these compounds, peptides with antihypertensive properties received special attention in the past 15 years. Although milk proteins are still the main source of antihypertensive peptides, recently a remarkable increase has been noticed in the report of antihypertensive peptides released from other dietary sources. Most of these peptides have demonstrated their properties by in vitro assays. However, the evidence for their beneficial antihypertensive effects has to be based on animal experiments and clinical trials. This paper reviews the current data of the blood pressure-lowering activity of food-derived peptides demonstrated in vivo (animal models and humans). Other aspects, such as the mechanism of action and bioavailability of these peptides which play a key role in their antihypertensive effects are also summarized in this review. This journal is © The Royal Society of Chemistry 2012