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A Very Short Route to Enantiomerically Pure Coumarin‐Bearing Fluorescent Amino Acids
Author(s) -
Brun MariePriscille,
Bischoff Laurent,
Garbay Christiane
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.200454116
Subject(s) - fluorescence , tyrosine , coumarin , tryptophan , amino acid , fluorescent labelling , chemistry , enantiomer , aromatic amino acids , residue (chemistry) , sequence (biology) , fluorescence microscope , confocal microscopy , biochemistry , stereochemistry , organic chemistry , biology , physics , quantum mechanics , microbiology and biotechnology
No bulkier than a tryptophan or a tyrosine residue are the fluorescent coumaryl amino acids described. These building blocks can be synthesized rapidly with high enantiomeric purity and introduced readily into a peptidic sequence. Their fluorescence properties allow, for example, the investigation of the cellular localization of labeled peptides through confocal fluorescence microscopy (see picture).