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

Alessandra Scotti, Claudio Trapella, Valeria Ferretti, Eleonora Gallerani, Riccardo Gavioli, Mauro Marastoni
2015 Journal of Enzyme Inhibition and Medicinal Chemistry  
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 mM range
more » ... of the post-acidic-like and chymotrypsin-like active sites of the proteasome.
doi:10.3109/14756366.2015.1037749 pmid:25942361 fatcat:365g3mlww5fq3cz6xsdpdhhrru