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- W4362458102 abstract "Chemical cross-linking mass spectrometry (CXMS) has emerged as a powerful technology to analyze protein complexes. However, the progress of in vivo CXMS studies has been limited by cross-linking biocompatibility and data analysis. Herein, a glycosidic bond-based MS-cleavable cross-linker of trehalose disuccinimidyl ester (TDS) was designed and synthesized, which was fragmented in MS under CID/HCD to simplify the cross-linked peptides into conventional single peptides via selective cleavage between glycosidic and peptide bonds under individual MS collision energy. Consequently, the cross-linking identification accuracy and throughput were significantly enhanced, and the popular MS mode of stepped HCD was allowed. In addition, TDS showed proper cell-penetrating properties while being highly water-soluble, making it non-DMSO dependent during solubilization. Collectively, TDS provides a promising toolkit for CXMS characterization of living systems with high biocompatibility and accuracy." @default.
- W4362458102 created "2023-04-05" @default.
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- W4362458102 date "2023-05-04" @default.
- W4362458102 modified "2023-10-17" @default.
- W4362458102 title "A Glycosidic‐Bond‐Based Mass‐Spectrometry‐Cleavable Cross‐linker Enables In Vivo Cross‐linking for Protein Complex Analysis" @default.
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- W4362458102 doi "https://doi.org/10.1002/anie.202212860" @default.
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