期刊
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 17, 期 3, 页码 649-653出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2006.10.100
关键词
activity-based probes; cysteine protease; fluorescent labeling; legumain
资金
- NCRR NIH HHS [U54 RR020843] Funding Source: Medline
- NIBIB NIH HHS [R01 EB005011, R01-EB005011] Funding Source: Medline
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. (c) 2006 Elsevier Ltd. All rights reserved.
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