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PTMC_The proteomic profiles of pyridinium-based strategy for lysine-selective protein modification in live cells

ABSTRACT: A new bioorthogonal lysine-labeling strategy based on cationic-pyridinium activated ester, which renders the modification of peptides and proteins’ lysine residues with ultrafast kinetics and excellent specificity under aqueous solution, and profiled reactive-lysine proteome in vitro and in live cells.

ORGANISM(S): Homo Sapiens

SUBMITTER: Zigang Li

PROVIDER: PXD036388 | iProX | Tue Oct 24 00:00:00 GMT+01:00 2023

REPOSITORIES: iProX

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A pyridinium-based strategy for lysine-selective protein modification and chemoproteomic profiling in live cells.

Wan Chuan C Yang Dongyan D Song Chunli C Liang Mingchan M An Yuhao Y Lian Chenshan C Dai Chuan C Ye Yuxin Y Yin Feng F Wang Rui R Li Zigang Z

Chemical science 20240313 14

Protein active states are dynamically regulated by various modifications; thus, endogenous protein modification is an important tool for understanding protein functions and networks in complicated biological systems. Here we developed a new pyridinium-based approach to label lysine residues under physiological conditions that is low-toxicity, efficient, and lysine-selective. Furthermore, we performed a large-scale analysis of the ∼70% lysine-selective proteome in MCF-7 cells using activity-based ...[more]

PMID: 38577373

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