Journal
BIOLOGICAL CHEMISTRY
Volume 401, Issue 1, Pages 165-182Publisher
WALTER DE GRUYTER GMBH
DOI: 10.1515/hsz-2019-0332
Keywords
activity-based probe; combinatorial peptide; library; protease reactive warhead; protease substrate; proteomics; substrate specificity
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Funding
- NIH [R01 EB026285 02]
- Swiss National Science Foundation [P2ELP3_155323 P300PB_164725]
- Stanford ChEM-H Chemistry/Biology Interface Predoctoral Training Program
- NSF Graduate Research Fellowship [DGE-114747]
- Stanford University
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Proteases are regulators of diverse biological pathways including protein catabolism, antigen processing and inflammation, as well as various disease conditions, such as malignant metastasis, viral infection and parasite invasion. The identification of substrates of a given protease is essential to understand its function and this information can also aid in the design of specific inhibitors and active site probes. However, the diversity of putative protein and peptide substrates makes connecting a protease to its downstream substrates technically difficult and time-consuming. To address this challenge in protease research, a range of methods have been developed to identify natural protein substrates as well as map the overall substrate specificity patterns of proteases. In this review, we highlight recent examples of both synthetic and biological methods that are being used to define the substrate specificity of protease so that new protease-specific tools and therapeutic agents can be developed.
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