Mercaptoacyl amino acid inhibitors of atriopeptidase. 1. Structure-activity relationship studies of methionine and S-alkylcysteine derivatives

J Med Chem. 1994 Jul 22;37(15):2461-76. doi: 10.1021/jm00041a026.

Abstract

A broad series of N-(3-mercaptoacyl) amino acid derivatives was evaluated for their ability to inhibit atriopeptidase (neutral endopeptidase, EC 3.4.24.11) in vitro and in vivo. Structural parameters studied were (i) the substituent on the 2-position of the 3-mercaptopropionyl moiety, (ii) the amino acid component, (iii) the S-terminal derivative, and (iv) the C-terminal derivative. Optimum activity was observed for derivatives of methionine and S-alkylcysteines. N-[3-Mercapto-2(S)-[(2-methylphenyl)methyl]-1-oxopropyl]-L-methionine was identified as a highly effective inhibitor of atriopeptidase meriting evaluation as a potential cardiovascular therapeutic agent.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / chemistry
  • Amino Acids / pharmacology*
  • Animals
  • Antihypertensive Agents / pharmacology*
  • Atrial Natriuretic Factor / pharmacology
  • Cholinesterase Inhibitors / pharmacology
  • Cysteine / analogs & derivatives*
  • Male
  • Methionine / chemistry*
  • Molecular Sequence Data
  • Neprilysin / antagonists & inhibitors*
  • Rats
  • Rats, Inbred SHR
  • Rats, Sprague-Dawley
  • Structure-Activity Relationship

Substances

  • Amino Acids
  • Antihypertensive Agents
  • Cholinesterase Inhibitors
  • Atrial Natriuretic Factor
  • Methionine
  • Neprilysin
  • Cysteine