Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 138, Issue 24, Pages 7472-7475Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.6b03390
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Funding
- Ruth L. Kirchstein National Service Award [NIH F31CA180696]
- Robert A. Welch Foundation [C-1680]
- National Science Foundation [CHB-1055569]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1055569] Funding Source: National Science Foundation
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Chemical modification of proteins and peptides represents a challenge of reaction design as well as an important biological tool. In contrast to side-chain modification, synthetic methods to alter backbone structure are extremely limited. In this communication, copper-mediated backbone N-alkenylation or N-arylation of peptides and proteins by direct modification of natural sequences is described. Histidine residues direct oxidative coupling of boronic acids at the backbone NH of a neighboring amino acid. The mild reaction conditions in common physiological buffers, at ambient temperature, are compatible with proteins and biological systems. This simple reaction demonstrates the potential for directed reactions in complex systems to allow modification of N-H bonds that directly affect polypeptide structure, stability, and function.
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