期刊
JOURNAL OF PEPTIDE SCIENCE
卷 11, 期 3, 页码 153-160出版社
WILEY
DOI: 10.1002/psc.608
关键词
fluorogenic substrates; fluorescent amino acids; coumarins; matrix metalloprotease activity
Two coumarin-labelled lysines were conveniently prepared as a fluorescence resonance energy transfer (FRET) pair for peptide cleavage detection. 7-Methoxy and 7-diethylamino coumarin-3-carboxylic acids were synthesized according to a modification of known procedures. Labelling at lysine was achieved in solution via the active N-hydroxysuccinimide ester of the carboxylic acid coumarin derivatives to give the target compounds in good yield. Subsequently, these modified amino acids were used in solid phase peptide synthesis (SPPS), and their potential utility in an extracellular matrix metalloprotease (MMP-1) activity measurement via FRET and/or quenching studies was demonstrated. Copyright (c) 2004 European Peptide Society and John Wiley T Sons, Ltd.
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