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