Development of lipopeptides for inhibiting 20S proteasomes.

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

https://www.ncbi.nlm.nih.gov/pubmed/16630721

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