α- and β-hydrazino acid-based pseudopeptides inhibit the chymotrypsin-like activity of the eukaryotic 20S proteasome
| Autor: | Andrea Bordessa, Massaba Keita, Jean-Louis Soulier, Cyril Bauvais, Sandrine Ongeri, Lucia Formicola, Guillaume Bernadat, Michèle Reboud-Ravaux, Benoit Crousse, Jordi Rodrigo, Laure Dufau, Thierry Milcent, Nathalie Lagarde, Xavier Maréchal |
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| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Stereochemistry Inhibitory postsynaptic potential 20s proteasome chemistry.chemical_compound Structure-Activity Relationship Drug Discovery Animals Chymotrypsin Chymotrypsin like Pharmacology Trifluoromethyl biology Dose-Response Relationship Drug Molecular Structure Chemistry Organic Chemistry General Medicine Hydrazines Proteasome Biochemistry biology.protein Rabbits Peptides Proteasome Inhibitors |
| Zdroj: | European journal of medicinal chemistry. 70 |
| ISSN: | 1768-3254 |
| Popis: | We describe the synthesis of a library of new pseudopeptides and their inhibitory activity of the rabbit 20S proteasome chymotrypsin-like (ChT-L) activity. We replaced a natural α-amino acid by an α- or a β-hydrazino acid and obtained inhibitors of proteasome up to a submicromolar range (0.7 μM for molecule 24b). Structural variations influenced the inhibition of the ChT-L activity. Models of inhibitor/20S proteasome complexes corroborated the inhibition efficacies obtained by kinetic studies. |
| Databáze: | OpenAIRE |
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