Renin inhibitors. Dipeptide analogs of angiotensinogen utilizing a structurally modified phenylalanine residue to impart proteolytic stability

JJ Plattner, PA Marcotte, HD Kleinert…

Index: Plattner; Marcotte; Kleinert; Stein; Greer; Bolis; Fung; Bopp; Luly; Sham; Kempf; Rosenberg; Dellaria; De; Merits; Perun Journal of Medicinal Chemistry, 1988 , vol. 31, # 12 p. 2277 - 2288

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Citation Number: 63

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. ...