Endogenous Cell-Surface Receptor Modification by Metal Chelation- Assisted Pyridinium Oxime Catalyst

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.

Automated summary

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.