EN
Five peptide renin inhibitors were synthesized and their potency was assayed in vitro by a spectrofluorometric method (assay of Leu-Val-Tyr-Ser released from N-acetyltetradecapeptide substrate by renin in the presence of an inhibitor). Their stability was tested by assay of Phe and Pro-Phe released after incubation with chymotrypsin. The most potent inhibitor was Boc-Phe-His-Sta-epsilonAhx-OME, the most stable - Boc-Pro-Phe-His-Sta-epsilonAhx-OME (resistant to incubation with chymotrypsin for 4 h).