A new fluorogenic peptide determines proteasome activity in single cells

Silvana A M Urru, Pietro Veglianese, Ada De Luigi, Elena Fumagalli, Eugenio Erba, Rodolfo Gonella Diaza, Andrea Carrà, Enrico Davoli, Tiziana Borsello, Gianluigi Forloni, Niccolò Pengo, Enrico Monzani, Paolo Cascio, Simone Cenci, Roberto Sitia, Mario Salmona

Research output: Contribution to journalArticlepeer-review


The ubiquitin-proteasome system plays a critical role in many diseases, making it an attractive biomarker and therapeutic target. However, the impact of results obtained in vitro using purified proteasome particles or whole cell extracts is limited by the lack of efficient methods to assess proteasome activity in living cells. We have engineered an internally quenched fluorogenic peptide with a proteasome-specific cleavage motif fused to TAT and linked to the fluorophores DABCYL and EDANS. This peptide penetrates cell membranes and is rapidly cleaved by the proteasomal chymotrypsin-like activity, generating a quantitative fluorescent reporter of in vivo proteasome activity as assessed by time-lapse or flow cytometry fluorescence analysis. This reporter is an innovative tool for monitoring proteasomal proteolytic activities in physiological and pathological conditions.

Original languageEnglish
Pages (from-to)7452-7460
Number of pages9
JournalJournal of Medicinal Chemistry
Issue number20
Publication statusPublished - Oct 28 2010

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery
  • Medicine(all)


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