Epoxysuccinyl peptide-derived affinity labels for cathepsin B |
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Authors: | Schaschke N Assfalg-Machleidt I Lassleben T Sommerhoff C P Moroder L Machleidt W |
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Affiliation: | Max-Planck-Institut für Biochemie, Martinsried, Germany. |
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Abstract: | Extracellular cysteine proteases, in particular cathepsin B, have been implicated in a variety of pathological processes. Selectively targeting labels of this enzyme are important tools to gain more detailed understanding of its specific roles. Starting from our recently developed irreversible epoxysuccinyl-based inhibitor (R-Gly-Gly-Leu-(2S,3S)-tEps-Leu-Pro-OH, R=OMe), we have synthesized two affinity labels, R=NH-(CH(2))(6)-NH-rhodamine B and R=NH-(CH(2))(6)-NH-biotin. Using MCF-7 cells, the labeled inhibitors were shown to be virtually non-cell-permeant. Moreover, affinity blot analysis with the biotinylated inhibitor allowed a highly sensitive and selective non-radioactive detection of active cathepsin B. |
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