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Current Strategies for Probing Substrate Specificity of Proteases

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In this review we describe in detail the available technologies used for investigating the substrate specificity of proteases. Critical comparison of the available detection methods and their choice for certain type of screening is discussed. We present successful strategies along with appropriate examples for the design and synthesis of combinatorial libraries of substrates using both chemical and biological approaches. Proteomic tools for the identification of natural substrates of proteases are also discussed.

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Keywords: 5-fluorosalicylic acid; 6-amino-1-naphtalenesulfonamide; 7-amino-4-carbamoylmethylcoumarin; 7-amino-4-methylcoumarin; 7-amino-4-trifluoromethylcoumarin; ABPs; ACC; AFC; AMC; AMCA; ANSN; Activity Based Probes; Leishmania mexicana; MEROPS; MMP-2; MT1-MMP; N-acyl-7-amino-4-methylcoumarin acetic acid; PICS; PROTOMAP; Protease; Proteomic Identification of protease Cleavage Sites; SAS; Tb(EDTA); Trypanasoma brucei; aspartic proteases; collagenase-3; combinatorial; cysteine proteases; fluorogenic; fsa; furin; granzyme B; iCat; iTRAQ; library; matrilysin; p-nitroanilide; pNA; positional scanning substrate combinatorial library; quencher; rhodesain; serine proteases; stromelysin; substrate; substrate activity screening; substrate specificity; thrombin

Document Type: Research Article

Publication date: 2010-01-01

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  • Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.
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