Matrix metalloproteinase inhibitors containing a (carboxyalkyl)amino zinc ligand: modification of the P1 and P2' residues
| Autor: | Peter Brown, David H. Drewry, Michael Foley, Chambers Cl, Frank Brown, Gregson M, Andrew B. McElroy, David N. Deaton, Davies Hg, Bickett Dm |
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| Rok vydání: | 1994 |
| Předmět: |
Indoles
Stereochemistry Matrix metalloproteinase inhibitor Molecular Sequence Data Substituent Isoindoles Matrix Metalloproteinase Inhibitors chemistry.chemical_compound Structure-Activity Relationship Drug Stability Drug Discovery Side chain medicine Humans Ethyl group Amino Acid Sequence Imide Fluorescent Dyes Dipeptide Molecular Structure Metalloendopeptidases Dipeptides Hydrogen-Ion Concentration Ligand (biochemistry) Extracellular Matrix Zinc chemistry Chromogenic Compounds Gelatinases Collagenase Molecular Medicine Matrix Metalloproteinase 3 medicine.drug Half-Life |
| Zdroj: | Journal of medicinal chemistry. 37(5) |
| ISSN: | 0022-2623 |
| Popis: | Systematic modification of the presumed P1 side chain in a series of (carboxyalkyl)amino-based inhibitors of matrix metalloproteinases enabled identification of the 2-(1,3-dihydro-1,3-dioxo-2H-benz [f]isoindol-2-yl)ethyl group as a preferred substituent imparting potent inhibition of the enzymes collagenase and gelatinase. It was subsequently found that the P2'-P3' residues in this series could be replaced by small non-peptide residues, while maintaining inhibitory potency. The imide group in this series of compounds can undergo autocatalytic hydrolysis under neutral conditions |
| Databáze: | OpenAIRE |
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