Journal
BIOLOGICAL CHEMISTRY
Volume 396, Issue 4, Pages 329-337Publisher
WALTER DE GRUYTER GMBH
DOI: 10.1515/hsz-2014-0315
Keywords
combinatorial library; endopeptidase; exopeptidase; fluorogenic substrates; unnatural amino acids
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Funding
- National Science Centre in Poland [2011/03/B/ST5/01048]
- Polish Ministry of Science and Higher Education for the Faculty of Chemistry at Wroclaw University of Technology
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Substrate specificity of proteases can be determined using several methods among which the most frequently used are positional scanning library, proteomics and phage display. Classic approaches can deliver information about preferences for natural amino acids in binding pockets of virtually all proteases. However, recent studies demonstrate the ability to obtain much more information by application of unnatural amino acids to positional scanning library approaches. This knowledge can be used for the design of more active and specific substrates, inhibitors and activity based probes. In this minireview we describe recent strategies and concepts for the design and application of fluorogenic substrates library tailored for exopeptidases and endopeptidases.
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