Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1377488 | Bioorganic & Medicinal Chemistry Letters | 2006 | 5 Pages |
Abstract
Proteasomes are responsible for the cytoplasmic turnover of the vast majority of proteins including regulatory proteins. We have synthesized lipopeptides a new class of non-covalent inhibitors of the 20S proteasome and assayed their inhibitory capacities. Their ability to inhibit at micromolar concentrations chymotrypsin-like and post-acid activities depends on peptide length (3 or 6 amino acids), sequence (presence of a positively or negatively charged amino acid), and alkyl chain length (C6-C18). These structural features could be varied to selectively inhibit one or more of the three proteasome activities.
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Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Nicolas Basse, David Papapostolou, Maurice Pagano, Michèle Reboud-Ravaux, Elise Bernard, Anne-Sophie Felten, Régis Vanderesse,