Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 54, Issue 15, Pages 4587-4591Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201411745
Keywords
bioorganic chemistry; diazo compounds; homogeneous catalysis; protein modifications; rhodium
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Funding
- NSF CAREER program [CHE1055569]
- Robert A. Welch Foundation [C-1680]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1055569] Funding Source: National Science Foundation
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Chemically modified proteins are increasingly important for use in fundamental biophysical studies, chemical biology, therapeutic protein development, and biomaterials. However, chemical methods typically produce heterogeneous labeling and cannot approach the exquisite selectivity of enzymatic reactions. While bioengineered methods are sometimes an option, selective reactions of natural proteins remain an unsolved problem. Here we show that rhodium(II) metallopeptides combine molecular recognition with promiscuous catalytic activity to allow covalent decoration of natural SH3 domains, depending on choice of catalyst but independent of the specific residue present. A metallopeptide catalyst succeeds in modifying a single SH3-containing kinase at endogenous concentrations in prostate cancer (PC-3) cell lysate.
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