基于邻近驱动的 N-磺酰基吡啶酮化学的活细胞蛋白磺酰化。
Live-Cell Protein Sulfonylation Based on Proximity-driven N-Sulfonyl Pyridone Chemistry.
机构信息
Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, 615-8510, Japan.
Present address: Research Institute for Electronic Science, Hokkaido University, N20, W10, Kita-Ku, Sapporo, Hokkaido, 001-0020, Japan.
出版信息
Angew Chem Int Ed Engl. 2018 Jan 15;57(3):659-662. doi: 10.1002/anie.201707972. Epub 2017 Dec 13.
The development of bioorthogonal approaches for labeling of endogenous proteins under the multimolecular crowding conditions of live cells is highly desirable for the analysis and engineering of proteins without using genetic manipulation. N-Sulfonyl pyridone (SP) is reported as a new reactive group for protein sulfonylation. The ligand-directed SP chemistry was able to modify not only purified proteins in vitro, but also endogenous ones on the surface of and inside live cells selectively and rapidly, which allowed to convert endogenous proteins to FRET-based biosensors in situ.
发展生物正交方法来标记活细胞中多种分子拥挤条件下的内源性蛋白质，对于在不进行遗传操作的情况下分析和工程化蛋白质是非常理想的。N-磺酰基吡啶酮（SP）被报道为一种新的蛋白质磺酰化反应基团。配体导向的 SP 化学不仅能够修饰体外的纯化蛋白质，还能够选择性和快速地修饰活细胞表面和内部的内源性蛋白质，从而能够将内源性蛋白质原位转化为基于 FRET 的生物传感器。
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