Ketomethyldipeptides I. A new class of angiotensin converting enzyme inhibitors
| Autor: | J.D. Godfrey, David W. Cushman, M.B. Rom, Eric M. Gordon, Harold N. Weller, Jelka Pluščec, Sesha I Natarajan, E. F. Sabo |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
chemistry.chemical_classification
Ketone biology Chemistry Stereochemistry Biophysics Substituent Substrate (chemistry) Angiotensin-converting enzyme Angiotensin-Converting Enzyme Inhibitors Stereoisomerism Cell Biology Tripeptide Dipeptides Biochemistry chemistry.chemical_compound Structure-Activity Relationship Enzyme Enzyme inhibitor biology.protein Binding site Molecular Biology Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 124(1) |
| ISSN: | 0006-291X |
| Popis: | The design rationale for a new series of angiotensin-converting enzyme (ACE) inhibitors which incorporate a ketone substituent into a peptide backbone is described. Molecular regions which were expected to mimic the binding of an N-acyl tripeptide substrate at secondary binding sites S 1 and S 1 ′ were systematically varied in order to study the specificity of inhibitor binding and optimize inhibition against ACE. The most effective ketomethyldipeptides inhibit ACE in the 10 −9 M range. |
| Databáze: | OpenAIRE |
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