BACKGROUND: Quinoa protein is a potential source of bioactive peptides. Although some studies have demonstrated its angiotensin converting enzyme (ACE) inhibitory properties, research into its in vivo effect on blood-pressure regulation and peptide characterization remains limited. RESULTS: Quinoa protein hydrolyzate (QPH) was prepared by simulated gastrointestinal digestion. QPH lowered the systolic blood pressure (SBP) and diastolic blood pressure (DBP) in spontaneously hypertensive model rats (SHRs) from 2 h to10 h after oral administration, effectively controlling blood pressure in these SHRs. An in vitro study showed that QPH is capable of inhibiting ACE activity. This was attributed to the activity of a number of low-molecular-weight peptides. With relatively high scores predicted by PeptideRanker, three promising bioactive peptides, FHPFPR, NWFPLPR, and NIFRPF, were further studied and their ACE-inhibition effects were confirmed with IC50 values of 34.92, 16.77, and 32.40 μM, respectively. A molecular docking study provided insights into the binding of ACE with peptides, and revealed that the presence of specific amino acids in the peptide sequence (Pro, Phe, and Arg at the C-terminal, and Asn at the N-terminal) could contribute to the interaction between ACE and peptides. CONCLUSION: These results demonstrated the potential of QPH for the management of hypertension, which indicates that it could be a good candidate for inclusion in functional foods to control high blood pressure.
BACKGROUND:Quinoa protein is a potential source of bioactive peptides. Although some studies have demonstrated its angiotensin converting enzyme (ACE) inhibitory properties, research into its in vivo effect on blood-pressure regulation and peptide characterization remains limited. RESULTS:Quinoa protein hydrolyzate (QPH) was prepared by simulated gastrointestinal digestion. QPH lowered the systolic blood pressure (SBP) and diastolic blood pressure (DBP) in spontaneously hypertensive model rats (SHRs) from 2 h to10 h after oral administration, effectively controlling blood pressure in these SHRs. An in vitro study showed that QPH is capable of inhibiting ACE activity. This was attributed to the activity of a number of low-molecular-weight peptides. With relatively high scores predicted by PeptideRanker, three promising bioactive peptides, FHPFPR, NWFPLPR, and NIFRPF, were further studied and their ACE-inhibition effects were confirmed with IC50 values of 34.92, 16.77, and 32.40 μM, respectively. A molecular docking study provided insights into the binding of ACE with peptides, and revealed that the presence of specific amino acids in the peptide sequence (Pro, Phe, and Arg at the C-terminal, and Asn at the N-terminal) could contribute to the interaction between ACE and peptides. CONCLUSION: These results demonstrated the potential of QPH for the management of hypertension, which indicates that it could be a good candidate for inclusion in functional foods to control high blood pressure.