Profiling primary protease specificity by peptide synthesis on a solid support

R H P  Doeze; B A  Maltman; C L  Egan; R V  Ulijn; S L  Flitsch

doi:10.1002/anie.200353367

Profiling primary protease specificity by peptide synthesis on a solid support

R H P Doeze, B A Maltman, C L Egan, R V Ulijn, S L Flitsch

Research output: Contribution to journal › Article › peer-review

26 Citations (Scopus)

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.

Original language	English
Pages (from-to)	3138-3141
Number of pages	4
Journal	Agewandte Chemie-International Edition
Volume	43
Issue number	24
DOIs	https://doi.org/10.1002/anie.200353367
Publication status	Published - 14 Jun 2004

Keywords

profiling
primary protease specificity
peptide synthesis
solid support
hydrolysis
substrate specificity
enzymes
fluorescent probe
high-throughput screening

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10.1002/anie.200353367

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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.",

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AU - Doeze, R H P

AU - Maltman, B A

AU - Egan, C L

AU - Ulijn, R V

AU - Flitsch, S L

PY - 2004/6/14

Y1 - 2004/6/14

N2 - 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.

AB - 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.

KW - profiling

KW - primary protease specificity

KW - peptide synthesis

KW - solid support

KW - hydrolysis

KW - substrate specificity

KW - enzymes

KW - fluorescent probe

KW - high-throughput screening

U2 - 10.1002/anie.200353367

DO - 10.1002/anie.200353367

M3 - Article

SN - 1433-7851

VL - 43

SP - 3138

EP - 3141

JO - Agewandte Chemie-International Edition

JF - Agewandte Chemie-International Edition

IS - 24

ER -

Profiling primary protease specificity by peptide synthesis on a solid support

Abstract

Keywords

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