Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1366959 | Bioorganic & Medicinal Chemistry Letters | 2007 | 5 Pages |
Abstract
A series of β-lactam derivatives has been designed and synthesized to inhibit the chymotrypsin-like activity of the human 20S proteasome. The most potent compounds of this new structural class of β-subunit selective 20S proteasome inhibitors exhibit IC50 values in the low-nanomolar range and show good selectivity over the trypsin-like and post-glutamyl-peptide hydrolytic activities of the enzyme.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Patricia Imbach, Marc Lang, Carlos García-Echeverría, Vito Guagnano, Maria Noorani, Johannes Roesel, Francis Bitsch, Grety Rihs, Pascal Furet,