Studies of C-terminal naphthoquinone dipeptides as 20S proteasome inhibitors

Abstract

The ubiquitin proteasome pathway is crucial in regulating many processes in the cell. Modulation of proteasome activities has emerged as a powerful strategy for potential therapies against much important pathologies. In particular, specific inhibitors may represent a useful tool for the treatment of tumors. Here, we report studies of a new series of peptide-based analogues bearing a naphthoquinone pharmacophoric unit at the C-terminal position. Some derivatives showed inhibition in the µM range of the post-acidic-like and chymotrypsin-like active sites of the proteasome.

• 20S Proteasome
• naphthoquinone derivatives
• pseudodipeptides
• synthetic inhibitor

Declaration of interest

The authors report no conflicts of interest. The authors alone are responsible for the content and writing of this article.