Chemoselective reactions allowing for amino acid-specific modification are essential for protein bioconjugation and covalent drug development. Apart from Lysine and Cysteine with superior nucleophilic side chains, other amino acid-selective reactions are also needed but not well developed. Herein, we report the development of the biocompatible and catalyst-free triazine-pyridine chemistry (TPC) for tyrosine-specific labelling under physiological conditions and profiling in whole proteome. TPC exhibited high tyrosine chemoselectivity in biological systems, displayed potentials in tyrosine-guided protein labelling, and had biocompatibility in living cells. The development of TPC based tyrosine labelling agents would offer additional tools in native protein chemical modification.
[doi:10.25345/C5Z231]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Tyrosine labeling, Triazine-pyridine chemistry
Principal Investigators: (in alphabetical order) |
Prof. Xuechen Li, The University of Hong Kong, China, HK |
Submitting User: | Sarah_2021 |
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