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

Georgios A Dalkas, Damien Marchand, Jean-Claude Galleyrand, Jean Martinez, Georgios A Spyroulias, Paul Cordopatis, Florine Cavelier

Department of Pharmacy, University of Patras, Panepistimioupoli-Rion, GR-26504, Greece.

Journal of peptide science : an official publication of the European Peptide Society 2010 Feb

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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.

Citation

Georgios A Dalkas, Damien Marchand, Jean-Claude Galleyrand, Jean Martinez, Georgios A Spyroulias, Paul Cordopatis, Florine Cavelier. Study of a lipophilic captopril analogue binding to angiotensin I converting enzyme. Journal of peptide science : an official publication of the European Peptide Society. 2010 Feb;16(2):91-7