Identification of renin inhibitors peptides from amaranth proteins by docking protocols

[Display omitted] •The application of adequate free software in identification of bioactive peptides is discussed.•New free, friendly and rigorous servers developed for docking with peptides were tested.•CABS-dock server was used to explore possible interaction sites on renin surface.•FlexPepDock server was used to estimate peptide-protein energy interaction.•FNLPILR peptide was identified as an inhibitor of the renin enzyme. The objective of this work was to develop a new protocol to predict with greater confidence peptides as potential inhibitors of the renin enzyme. For this, free, friendly and rigorous servers developed specifically for peptides as ligands were used. Six peptides (SFNLPILR; FNLPILR; SFNLPIL; QAFEDGFEWVSFK; AFEDGFEWVSFK and VNVDDPSKA) identified in an amaranth hydrolysate obtained with alcalase (hydrolysis degree 21% ± 4) were used. Two positive (angiotensinogen and IRLIIVLMPILMA) and one negative (a tridecapeptide of alanine) controls were included in the analysis. A protocol was designed to include two consecutive stages was performed using CABS-dock server (http://biocomp.chem.uw.edu.pl/CABSdock) and FlexPepDock server (http://flexpepdock.furmanlab.cs.huji.ac.il/). Peptides SFNLPILR, FNLPILR and AFEDGFEWVSFK inhibited the enzyme in vitro. The heptapeptide FNLPILR was the most potent inhibitor, with an IC50 of 0.41 mM.