Ketomethylureas. A new class of angiotensin converting enzyme inhibitors
| Autor: | J.D. Godfrey, Jack M. DeForrest, Jelka Pluščec, E. F. Sabo, M.B. Rom, J. Engebrecht, Sesha I Natarajan, Eric M. Gordon, Harold N. Weller, David W. Cushman, J. Powell |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Methylurea Compounds
biology Chemistry Stereochemistry Angiotensin-converting enzyme Angiotensin-Converting Enzyme Inhibitors Tripeptide Ketones Biochemistry Rats Kinetics Structure-Activity Relationship Nitrogen atom Asymmetric carbon biology.protein Molecular Medicine Peptide bond Animals Indicators and Reagents Amino acid residue Oligopeptides |
| Zdroj: | Journal of enzyme inhibition. 2(2) |
| ISSN: | 8755-5093 |
| Popis: | The design rationale for a new series of tripeptide derived angiotensin converting enzyme (ACE) inhibitors, which we term “ketomethylureas”, is described. Analogs of tripeptide substrates (i.e. N-benzoyl-Phe-Ala-Pro) in which the nitrogen atom of the scissile amide bond and the adjacent asymmetric carbon atom of the penultimate amino acid residue are formally transposed give rise to this novel class of inhibitors. The most potent ketomethylureas inhibit ACE wtih I50 values in the nM range. |
| Databáze: | OpenAIRE |
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