Development of lipopeptides for inhibiting 20S proteasomes.
Fiche publication
Date publication
juin 2006
Auteurs
Membres identifiés du Cancéropôle Est :
Dr VANDERESSE Régis
Tous les auteurs :
Basse N, Papapostolou D, Pagano M, Reboud-Ravaux M, Bernard E, Felten AS, Vanderesse R
Lien Pubmed
Résumé
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.
Référence
Bioorg Med Chem Lett. 2006 Jun 15;16(12):3277-81