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 1521-3773 (https://doi.org/10.1002/anie.200353367)
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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.
ORCID iDs
Doeze, R H P, Maltman, B A, Egan, C L, Ulijn, R V ORCID: https://orcid.org/0000-0001-7974-3779 and Flitsch, S L;-
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Item type: Article ID code: 43940 Dates: DateEvent14 June 2004PublishedSubjects: Science > Chemistry
Medicine > Pharmacy and materia medicaDepartment: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Faculty of Science > Pure and Applied ChemistryDepositing user: Pure Administrator Date deposited: 30 May 2013 11:23 Last modified: 11 Nov 2024 10:25 URI: https://strathprints.strath.ac.uk/id/eprint/43940