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

Article Details

Citation

Copy to clipboard

Dalkas GA, Marchand D, Galleyrand JC, Martinez J, Spyroulias GA, Cordopatis P, Cavelier F

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.

PubMed ID

20014331 [ View in PubMed

]

Abstract

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.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Captopril	Angiotensin-converting enzyme	Protein	Humans	Yes	Inhibitor	Details