期刊
JACS AU
卷 1, 期 7, 页码 1066-1075出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacsau.1c00172
关键词
biocompatible reaction; visible light photocatalysis; protein labeling; live cells; mitochondria
资金
- National Natural Science Foundation of China [91753126, 21622207, 21602242, 31671428, 31530041]
- CAS Interdisciplinary Innovation Team [JCTD-2020-16]
- National Key R&D Program of China [2016YFA0501904, 2016YFA0501900]
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDB20020200]
- Shanghai Municipal Science and Technology Major Project [2019SHZDZX02]
Biocompatible photocatalytic azide conjugation reaction enables selective labeling of mitochondrial proteins inside live cells, mapping dynamic mitochondrial proteome changes with high temporal-spatial precision.
Biocompatible reactions are powerful tools to probe protein functions in their native environment. Due to the difficulty of penetrating the live-cell membrane and the complex intracellular environment, the biocompatible reactions inside live cells are challenging, especially at the subcellular level with spatial resolution. Here we report the first biocompatible photocatalytic azide conjugation reaction inside live cells to achieve the mitochondria-selective proteins labeling. The organic dyes acridine orange, fluorescein, and rhodamine 123 were developed as the biocompatible photocatalysts for the proteins labeling with aryl azides, which yielded benzazirines and ketenimines from triplet nitrenes for the protein nucleophilic residue trapping. The photocatalytic azide conjugation reaction with rhodamine 123 selectively labeled the mitochondrial proteins via the organic dye's mitochondrial localization. In response to the mitochondrial stress induced by rotenone, this photocatalytic azide-promoted labeling method mapped the dynamic mitochondrial proteome changes with high temporal-spatial precision and identified several potential mitochondrial stress-response proteins for the first time. The high temporal-spatial precision of this photocatalytic azide-promoted labeling method holds excellent potential for intracellular protein network investigations.
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