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Profiling primary protease specificity by peptide synthesis on a solid support

Doeze, R H P and Maltman, B A and Egan, C L and Ulijn, R V and Flitsch, S L (2004) Profiling primary protease specificity by peptide synthesis on a solid support. Agewandte Chemie-International Edition, 43 (24). pp. 3138-3141. ISSN 1433-7851

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Abstract

Reverse screening: A greatly simplified primary screening of protease specificity has been achieved by monitoring the fluorescence during the protease-catalyzed coupling of amino acids instead of peptide hydrolysis on a solid support (see picture, AA=amino acid). This approach paves the way for flexible, rapid, high-throughput identification and characterization of proteases without the need for expensively labeled peptide arrays.

Item type: Article
ID code: 43940
Keywords: profiling, primary protease specificity, peptide synthesis, solid support, hydrolysis, substrate specificity, enzymes, fluorescent probe, high-throughput screening, Chemistry, Pharmacy and materia medica, Chemistry(all), Catalysis
Subjects: Science > Chemistry
Medicine > Pharmacy and materia medica
Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Faculty of Science > Pure and Applied Chemistry
Depositing user: Pure Administrator
Date deposited: 30 May 2013 11:23
Last modified: 03 Jan 2019 13:45
URI: https://strathprints.strath.ac.uk/id/eprint/43940
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