Identification of novel renin inhibitory peptides from tartary buckwheat albumin hydrolysates by molecular docking

In contrast to the inhibition of angiotensin-converting enzyme (ACE), inhibition of renin activity controls increases in blood pressure at the source. Few renin inhibitory peptides have been reported. In this study, novel renin inhibitory peptides were identified from tartary buckwheat albumin hydrolysates (TBAHs). The structural characteristics of the peptide fractions with renin inhibitory activity in TBAHs were investigated by column separation. The potential renin inhibitory peptides were screened and the interactions of the peptides with renin were investigated by molecular docking. The peptides fractions with more charge and hydrophobicity were found to have a greater inhibitory effect on renin. After the screening, seven peptides were selected and synthesized, all of which showed renin inhibitory activity. The IC50 values of the peptides LFFR and LGLLPYFR were 5.00 mM and 10.19 mM,which both contained leucine (L) at the N-terminus and arginine (R) at the C-terminus. The molecular docking analysis indicated that the peptides interact with the active center of renin mainly by hydrophobic interactions. This was the first study to isolate renin inhibitory peptides from tartary buckwheat.