[Synthesis of angiotensin converting enzyme inhibitors containing residues of substituted quinolines and a study of their biological activity].

Inhibitors of the angiotensin-converting enzyme were synthesized by substituting N-and C-terminal amino acid residues of tripeptide Bz-Phe-Ala-Pro by the residues of 8-methoxy-5-sulphoquinoline and carboxy-1,2,3,4-tetrahydroquinoline, respectively, and their in vivo and in vitro biological activity was determined. The enzyme's S2' site proved to be non specific to the position of the carboxylic group in the C-terminal heterocyclic part of the inhibitor molecule. Introducing a modified quinoline residue into the N-terminal part of the inhibitor does not increase its specific interaction with the hydrophobic pocket of the angiotensin-converting enzyme.