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Profiling Primary Protease Specificity by Peptide Synthesis on a Solid Support
Author(s) -
Doezé Ron H. P.,
Maltman Beatrice A.,
Egan Claire L.,
Ulijn Rein V.,
Flitsch Sabine L.
Publication year - 2004
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200353367
Subject(s) - protease , proteases , peptide , amino acid , chemistry , biochemistry , combinatorial chemistry , hydrolysis , enzyme , computational biology , biology
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.