string(19) "en/achievements/739" Global profiling of arginine reactivity and ligandability in the human proteome-Shenzhen Medical Academy of Research and Translation
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Global profiling of arginine reactivity and ligandability in the human proteome

Date：2022/02/09

Source：深圳医学科学院

This Nature Chemistry paper reports the first proteome-wide mapping of arginine reactivity and ligandability in human cells using phenylglyoxal (PG)-based ABPP probes. The authors optimized PG derivatives to boost selectivity and coverage, identifying 4,606 arginine sites across multiple human cell lines.


Using on-beads reductive dimethylation proteomics, they defined hyper-reactive arginine residues linked to enzyme active sites and protein function. Competitive fragment screening with 60 dicarbonyl compounds via DIA-ABPP yielded a ligandability map, revealing ligandable arginines that modulate enzyme activity and protein-protein interactions (PPIs).


This study used the SCIEX QTRAP 7500+ in the Multi-omics Mass Spectrometry Core Facility of SMART Bio-Tech Center for smallmolecule quantification to measure intracellular dynamic levels of probes with arginine ligandability.

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