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.

Creators(s): Doeze, R H P, Maltman, B A, Egan, C L, Ulijn, R V ORCID logoORCID: https://orcid.org/0000-0001-7974-3779 and Flitsch, S L;
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:20 Jan 2021 20:42
URI:https://strathprints.strath.ac.uk/id/eprint/43940
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