Selective Activity-Based Probes for Cysteine Cathepsins (pages 406–409)
Anja Watzke, Gregor Kosec, Maik Kindermann, Volker Jeske, Hans-Peter Nestler, Vito Turk, Boris Turk and K. Ulrich Wendt
Version of Record online: 19 NOV 2007 | DOI: 10.1002/anie.200702811
By “reverse design”: The core structures of protease inhibitors, whose selectivity has been optimized by extensive medicinal chemistry, have been redesigned into selective protease substrates by replacing the reactive electrophilic group (e.g. nitrile) with a cleavable peptide bond. Attachment of appropriate reporter groups yields cell-permeable activity-based probes for the cellular imaging of selected cysteine cathepsins.