Live-Cell Protein Sulfonylation Based on Proximity-driven N-Sulfonyl Pyridone Chemistry

Kazuya Matsuo; Yuki Nishikawa; Marie Masuda; Itaru Hamachi

doi:10.1002/anie.201707972

Live-Cell Protein Sulfonylation Based on Proximity-driven N-Sulfonyl Pyridone Chemistry

Angew Chem Int Ed Engl. 2018 Jan 15;57(3):659-662. doi: 10.1002/anie.201707972. Epub 2017 Dec 13.

Authors

Kazuya Matsuo^{1

2}, Yuki Nishikawa¹, Marie Masuda¹, Itaru Hamachi^{1

3}

Affiliations

¹ Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, 615-8510, Japan.
² Present address: Research Institute for Electronic Science, Hokkaido University, N20, W10, Kita-Ku, Sapporo, Hokkaido, 001-0020, Japan.
³ Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST), 5 Sanbancho, Chiyoda-ku, Tokyo, 102-0075, Japan.

PMID: 29193552
DOI: 10.1002/anie.201707972

Abstract

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.

Keywords: FRET biosensors; N-sulfonyl pyridones; intracellular protein labeling; traceless affinity sulfonylation.

Publication types

Research Support, Non-U.S. Gov't