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Renin inhibitors. Dipeptide analogues of angiotensinogen utilizing a structurally modified phenylalanine residue to
J J Plattner1, P A Marcotte, H D Kleinert
1Abbott Laboratories, Pharmaceutical Discovery Division, Abbott Park, Illinois 60064.
Journal of Medicinal Chemistry
|December 1, 1988
Abstract:
A series of renin inhibitors have been prepared and evaluated for their susceptibility to cleavage by the serine protease chymotrypsin. The compounds were designed by consideration of the structural requirements in the active-site region of renin and chymotrypsin. By systematic alteration of the P3 phenylalanine residue, compounds with varying degrees of renin inhibitory potency and chymotrypsin susceptibility were obtained. Selected analogues from this group were examined in vivo for both their hypotensive effects and metabolic patterns.