Design of cell-permeable, fluorescent activity-based probes for the lysosomal cysteine protease asparaginyl endopeptidase (AEP)/legumain

Kelly B. Sexton, Martin D. Witte, Galia Blum, Matthew Bogyo

Research output: Contribution to journalArticleAcademic

32 Citations (Scopus)
25 Downloads (Pure)


Asparaginyl endopeptidase (AEP), also known as legumain, is a cysteine protease that has been ascribed roles in antigen presentation yet its exact role in human biology remains poorly understood. We report here, the use of a positional scanning combinatorial library of peptide AOMKs containing a P1 aspartic acid to probe the P2, P3, and P4 subsite specificity of endogenous legumain. Using inhibitor specificity profiles of cathepsin B and legumain, we designed fluorescent ABPs that are highly selective, cell-permeable reagents for monitoring legumain activity in complex proteomes.
Original languageEnglish
Pages (from-to)649-653
Number of pages5
JournalBioorganic & Medicinal Chemistry Letters
Issue number3
Publication statusPublished - 2007


  • Legumain
  • Fluorescent labeling
  • Cysteine protease
  • Activity-based probes

Cite this