Journal
ORGANIC LETTERS
Volume 25, Issue 12, Pages 2118-2122Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.orglett.3c00541
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The His-tag/NiNTA interaction promotes a new catalytic protein acylation strategy, enabling selective protein labeling in biological milieu. The recognition-assisted activation mechanism allows for efficient protein labeling at lower substrate concentrations, enabling highly selective and efficient cell-surface receptor modification in live cells.
Organocatalyst-mediated acyl transfer reactions hold promise for selective protein labeling in biological milieu. However, they often suffer from off-target reactions and high background signals because of the requirement of high concentrations of substrates. Here, we report a new catalytic protein acylation strategy promoted by the His-tag/NiNTA interaction. The recognition-assisted activation mechanism allows efficient protein labeling even with >10-fold lower substrate concentrations than conventional reactions, thereby enabling highly selective and efficient cell-surface receptor modification in live cells.
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