Journal
CHEMICAL COMMUNICATIONS
Volume 55, Issue 19, Pages 2841-2844Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9cc00159j
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Funding
- Robert A. Welch Foundation [C-1680]
- National Science Foundation [CHE-1055569]
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S-Arylation of cysteine residues is an increasingly powerful tool for site-specific modification of proteins, providing novel structure and electronic perturbation. The present work demonstrates an operationally-simple cysteine arylation reaction 2-nitro-substituted arylboronic acids, promoted by a simple nickel(ii) salt. The process exhibits strikingly fast reaction rates under physiological conditions in purely aqueous media with excellent selectivity toward cysteine residues. Cysteine arylation of natural proteins and peptides allows attachment of useful reactive handles for stapling, imaging, or further conjugation.
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