Design of Cell-permeable, Fluorescent Activity-based Probes for the Lysosomal Cysteine Protease Asparaginyl Endopeptidase (AEP)/legumain

Overview

Journal Bioorg Med Chem Lett

Specialty Biochemistry

Date 2006 Dec 27

PMID 17189693

Citations 25

Authors

Kelly B Sexton

Martin D Witte

Galia Blum

Matthew Bogyo

Affiliations

Soon will be listed here.

Abstract

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.

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