Profiling Primary Protease Specificity by Peptide Synthesis on a Solid Support

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 flex...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2004-06, Vol.43 (24), p.3138-3141
Main Authors: Doezé, Ron H. P., Maltman, Beatrice A., Egan, Claire L., Ulijn, Rein V., Flitsch, Sabine L.
Format: Article
Language:English
Subjects:
Acrylamides
Amino Acids - chemistry
Bacillus - enzymology
Biocompatible Materials
enzymes
fluorescent probes
high-throughput screening
hydrolysis
Peptide Hydrolases - chemistry
Peptides - chemical synthesis
Polyethylene Glycols
Polymers
Substrate Specificity
Thermolysin - chemistry
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Summary: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200353367