Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 53, Issue 44, Pages 11955-11959Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201406909
Keywords
excimers; fluorescent probes; peptide nucleic acids; proteases; time-resolved fluorescence
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Funding
- Federal Institute for Materials Research and Testing
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Peptide-based probes that fluoresce upon proteolytic cleavage are invaluable tools for monitoring protease activity. The read-out of protease activity through pyrene excimer signaling would be a valuable asset because the large Stokes shift and the long lifetime of the excimer emission facilitate measurements in autofluorescent media such as blood serum. However, proteolytic cleavage abolishes rather than installs the proximity relationships required for excimer signaling. Herein, we introduce a new probe architecture to enable the switching on of pyrene excimer emission upon proteolytic scission. The method relies on hairpin-structured peptide nucleic acid (PNA)/peptide hybrids with pyrene units and anthraquinone-based quencher residues positioned in a zipper-like arrangement within the PNA stem. The excimer hairpin peptide beacons afforded up to a 50-fold enhancement of the pyrene excimer emission. Time-resolved measurements allowed the detection of matrix metalloprotease 7 in human blood serum.
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