Development of lipopeptides for inhibiting 20S proteasomes

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• 作者：Nicolas Basse ; David Papapostolou ; Maurice Pagano ; Michè ; le Reboud-Ravaux ; Elise Bernard ; Anne-Sophie Felten and Ré ; gis Vanderesse
• 关键词：Proteasome ; Inhibitors ; Lipopeptides
• 刊名：Bioorganic and Medicinal Chemistry Letters
• 出版年：2006
• 出版时间：15 June 2006
• 年：2006
• 卷：16
• 期：12
• 页码：3277-3281
• 全文大小：197 K

文摘

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.