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Highly Sensitive Protease Assay Using Fluorescence Quenching of Peptide Probes Based on Photoinduced Electron Transfer
Author(s) -
Marmé Nicole,
Knemeyer JensPeter,
Wolfrum Jürgen,
Sauer Markus
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.200453835
Subject(s) - fluorophore , fluorescence , tryptophan , quenching (fluorescence) , chemistry , peptide , electron transfer , photochemistry , protease , cleavage (geology) , biophysics , photoinduced electron transfer , enzyme , biochemistry , materials science , biology , amino acid , optics , physics , fracture (geology) , composite material
Making the cut and then detecting it : Short fluorophore‐labeled peptide substrates (see scheme) show strong fluorescence quenching due to electron transfer from a tryptophan residue (blue) to the dye (gray, red). Upon specific cleavage of the peptide by proteolytic enzymes, quenching is prevented and the fluorescence intensity increases. The method can be used to assay proteolytic enzymes with detection limits in the picomolar range.