Molecular docking of the peptides at ACE and renin active sites.

<p>Results of peptide-ACE interactions are showed in A (TF), B (LY), C (RALP), and that of peptide-renin interactions are D (TF), E (LY), F (RALP). Enzyme hydrophobic residues are represented in red, positively charged residues are represented in blue, negatively charged residues and hydrogen bonds are represented in green, and other residues are represented automatically. (Image obtained with Accelrys DS Visualizer software).