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Bioorg Med Chem. 2009 Feb 1;17(3):1094-100. doi: 10.1016/j.bmc.2008.03.068. Epub 2008 Mar 30.

Using specificity to strategically target proteases.

Author information

1
Department of Pharmaceutical Chemistry, University of California, School of Pharmacy, 513 Parnassus Avenue Room S-926, San Francisco, CA 94158, USA.

Abstract

Proteases are a family of naturally occurring enzymes in the body whose dysregulation has been implicated in numerous diseases and cancers. Their ability to selectively and catalytically turnover substrate adds both signal amplification and functionality as parameters for the detection of disease. This review will focus on the development of activity-based methodologies to characterize proteases, and in particular, the use of positional scanning, synthetic combinatorial libraries (PS-SCL's), and substrate activity screening (SAS) assays. The use of these approaches to better understand a protease's natural substrate will be discussed as well as the technologies that emerged.

PMID:
18434168
PMCID:
PMC2663002
DOI:
10.1016/j.bmc.2008.03.068
[Indexed for MEDLINE]
Free PMC Article

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