Synthesis and studies of biological activity of inhibitors of the angiotensin-converting enzyme, containing residues of substituted quinolines

M. P. Filatova, N. A. Krit, N. N. Uskova, E. M. Maksimova, I. N. Gracheva, S. Reissmann

Institute of Biological and Medical Chemistry, Academy of Medical Sciences of the USSR, Moscow; F. Schiller University, Iena, GDR

Abstract: 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-l,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 hetero-cyclic 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 hydro-phobic pocket of the angiotensin-converting enzyme.

Russian Journal of Bioorganic Chemistry 1991, 17 (5):690-696

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