Novel ketomethylene inhibitors of angiotensin I-converting enzyme (ACE): inhibition and molecular modelling

Biol Chem. 2006 Apr;387(4):461-6. doi: 10.1515/BC.2006.061.

Abstract

Inhibition of angiotensin I-converting enzyme (ACE) has become an effective strategy in the treatment of hypertension and cardiovascular disease. Keto-ACE, a previously described C-domain selective ACE inhibitor, was used as the basis for the design, synthesis and molecular modelling of a series of novel ketomethylene derivatives for which ACE inhibition profiles and structural characterisation are reported. Ki determinations indicated that the introduction of a bulky aromatic tryptophan at the P2' position of keto-ACE significantly increased selectivity for the C-domain, while an aliphatic P2 Boc group conferred N-domain selectivity. These data were supported by the potential energies of the compounds docked with the C- and N-domains of ACE.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors / chemistry*
  • Angiotensin-Converting Enzyme Inhibitors / pharmacology*
  • Computer Simulation
  • Humans
  • Kinetics
  • Models, Molecular*
  • Peptidyl-Dipeptidase A / chemistry*
  • Protein Structure, Tertiary
  • Structure-Activity Relationship

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Peptidyl-Dipeptidase A