Journal
SCIENCE
Volume 355, Issue 6325, Pages 597-602Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aal3316
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Funding
- U.S. Department of Energy/Lawrence Berkeley National Laboratory [101528-002, DE-AC02-05CH11231]
- NIH [1S10OD020062-01, F32CA203152]
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Cysteine can be specifically functionalized by a myriad of acid-base conjugation strategies for applications ranging from probing protein function to antibody-drug conjugates and proteomics. In contrast, selective ligation to the other sulfur-containing amino acid, methionine, has been precluded by its intrinsically weaker nucleophilicity. Here, we report a strategy for chemoselective methionine bioconjugation through redox reactivity, using oxaziridine-based reagents to achieve highly selective, rapid, and robust methionine labeling under a range of biocompatible reaction conditions. We highlight the broad utility of this conjugation method to enable precise addition of payloads to proteins, synthesis of antibody-drug conjugates, and identification of hyperreactive methionine residues in whole proteomes.
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