title: Using specificity to strategically target proteases.
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.
authors.affiliation: Department of Pharmaceutical Chemistry, University of California, School of Pharmacy, 513 Parnassus Avenue Room S-926, San Francisco, CA 94158, USA.
authors.forename: Mark D
authors.initials: MD
authors.lastname: Lim
authors.forename: Charles S
authors.initials: CS
authors.lastname: Craik
mesh_terms: D020650:Combinatorial Chemistry Techniques; D015335:Molecular Probes; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000378:metabolism; D019151:Peptide Library; D011480:Protease Inhibitors / Q000138:chemical synthesis / Q000737:chemistry*; D054852:Small Molecule Libraries; D013379:Substrate Specificity
chemical_list: D015335:Molecular Probes; D019151:Peptide Library; D011480:Protease Inhibitors; D054852:Small Molecule Libraries; D010447:Peptide Hydrolases