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Live‐Cell Protein Sulfonylation Based on Proximity‐driven N ‐Sulfonyl Pyridone Chemistry
Author(s) -
Matsuo Kazuya,
Nishikawa Yuki,
Masuda Marie,
Hamachi Itaru
Publication year - 2018
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201707972
Subject(s) - bioorthogonal chemistry , endogeny , chemistry , in vitro , protein engineering , sulfonyl , ligand (biochemistry) , biosensor , biochemistry , enzyme , combinatorial chemistry , click chemistry , organic chemistry , receptor , alkyl
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.