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Article Dans Une Revue Journal of Peptide Science Année : 2010

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

Résumé

HumanACE is a central component of the renin–angiotensin systemand amajor 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.

Domaines

Chimie organique

Dates et versions

hal-00449420 , version 1 (21-01-2010)

Identifiants

Citer

Georgios A. Dalkas, Damien Marchand, Jean-Claude Galleyrand, Jean Martinez, Georgios A. Spyroulias, et al.. Study of a lipophilic captopril analogue binding to angiotensin I converting enzyme. Journal of Peptide Science, 2010, 16, pp.91-97. ⟨10.1002/psc.1201⟩. ⟨hal-00449420⟩
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