Configuration and preferential solid-state conformations of perindoprilat (S-9780). Comparison with the crystal structures of other ACE inhibitors and conclusions related to structure-activity relationships.
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Pascard C, Guilhem J, Vincent M, Remond G, Portevin B, Laubie M
Configuration and preferential solid-state conformations of perindoprilat (S-9780). Comparison with the crystal structures of other ACE inhibitors and conclusions related to structure-activity relationships.
J Med Chem. 1991 Feb;34(2):663-9.
- PubMed ID
- 1995891 [ View in PubMed]
- Abstract
The conformation of perindoprilat, an antihypertensive drug, is studied in the solid state by X-ray analysis. The resolution of its structure reveals important analogies between its observed conformation and that of several ACE inhibitors of the same family. This comparison points out a constant relative orientation of the functional groups, regardless of the molecular environment. This angular constancy appears to us as not being accidental and is a good argument for the spatial design of the ACE binding site. Although ACE is a carboxydipeptidase, the binding site may not contain two but one unique hydrophobic pocket receiving the C-terminal end of the inhibitors.
DrugBank Data that Cites this Article
- Binding Properties
Drug Target Property Measurement pH Temperature (°C) Epicaptopril Angiotensin-converting enzyme IC 50 (nM) 1.5 N/A N/A Details Epicaptopril Angiotensin-converting enzyme IC 50 (nM) 23 N/A N/A Details