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Updated: May 6, 2026
Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling
Published on: September 20, 2016
Development of Nuclear-Targeted Photoaffinity Probes with Cleavable Disulfide Bonds for Enhancing Selectivity in hPTM
Bei-Chen Wang1, Shuo Yang1, Fang-Hui Chen1
1School of Food and Biological Engineering, Engineering Research Center of Bio-process, Ministry of Education, Key Laboratory of Animal Source of Anhui Province, Hefei University of Technology, Hefei 230009, China.
Abstract:
Cell-penetrating, nuclear-targeted histone photoaffinity probes enable histone post-translational modification (hPTM) interactome profiling in native cells, yet noncleavable cell-penetrating peptides (e.g., cyclic polyarginine cell-penetrating peptide, cR10) induce interference due to their high positive charge. Herein, via facile synthesis, we developed novel nuclear-targeted histone photoaffinity probes with intracellularly cleavable cR10-disulfide linkages, targeting H3K4me3/H3K14la. In vitro labeling and proteomic assays demonstrated significantly improved binding selectivity for reader proteins and drastically reduced false-positive signals following cR10 cleavage.
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