Fischbach, Melanie published the artcileProtease Probes that Enable Excimer Signaling upon Scission, SDS of cas: 186046-83-3, the publication is Angewandte Chemie, International Edition (2014), 53(44), 11955-11959, database is CAplus and MEDLINE.
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 relations required for excimer signaling. Herein, the authors 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.
Angewandte Chemie, International Edition published new progress about 186046-83-3. 186046-83-3 belongs to amides-buliding-blocks, auxiliary class Purine,Carboxylic acid,Amine,Benzene,Amide,Others,PNA,, name is 2-(N-(2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)ethyl)-2-(2-(((benzhydryloxy)carbonyl)amino)-6-oxo-5H-purin-9(6H)-yl)acetamido)acetic acid, and the molecular formula is C40H35N7O8, SDS of cas: 186046-83-3.
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