Study of a lipophilic captopril analogue binding to angiotensin I converting enzyme

J Pept Sci. 2010 Feb;16(2):91-7. doi: 10.1002/psc.1201.


Human ACE is a central component of the renin-angiotensin system and a major therapeutic target for cardiovascular diseases. The somatic form of the enzyme (sACE) comprises two homologous metallopeptidase domains (N and C), each bearing a zinc active site with similar but distinct substrate and inhibitor specificities. In this study, we present the biological activity of silacaptopril, a silylated analogue of captopril, and its binding affinity towards ACE. Based on the recently determined crystal structures of both the ACE domains, a series of docking calculations were carried out in order to study the structural characteristics and the binding properties of silacaptopril and its analogues with ACE.

MeSH terms

  • Captopril / analogs & derivatives*
  • Captopril / chemistry
  • Captopril / metabolism
  • Catalytic Domain
  • Computer Simulation
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / metabolism
  • Humans
  • Inhibitory Concentration 50
  • Molecular Structure
  • Organosilicon Compounds / chemistry*
  • Organosilicon Compounds / metabolism*
  • Peptidyl-Dipeptidase A / chemistry
  • Peptidyl-Dipeptidase A / metabolism*
  • Protein Binding


  • Enzyme Inhibitors
  • Organosilicon Compounds
  • silacaptopril
  • Captopril
  • Peptidyl-Dipeptidase A