Tyrosine bioconjugation using stably preparable urazole radicals

<h2>Abstract</h2> Our <i>ex situ</i> tyrosine bioconjugation method utilizes the oxidation of <i>N</i>-methylurazole by Bobbitt's salt or electrochemical activation to generate stable radicals for selective tyrosine labeling, thereby addressing the longstanding challenges in protein bioconjugation. Unlike traditional tyrosine conjugation techniques that rely on closed-shell chemistry with 1,2,4-triazoline-3,5-dione derivatives, this method introduces an alternative bond-forming mechanism that expands bioconjugation through a radical-based pathway that enhances tyrosine selectivity. The applicability of this method was demonstrated for various proteins and validated through proteome-wide analyses, highlighting its potential as a valuable tool for investigating protein function and interaction dynamics.

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Publication Details

Journal
Tetrahedron Chem
Published
2024-11-19
DOI
https://doi.org/10.1016/j.tchem.2024.100111
Citations
2
Primary Topic
Click Chemistry and Applications
Type
article
Field-Weighted Citation Impact
0.50

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article

Tyrosine bioconjugation using stably preparable urazole radicals

Chizu Fujimura, Munehiro Kumashiro, Tomohide Saio, Shogo Miyano et al.
2 citations
Tetrahedron Chem
Click Chemistry and Applications
0.50
article

Tyrosine bioconjugation using stably preparable urazole radicals

Chizu Fujimura, Munehiro Kumashiro, Tomohide Saio, Shogo Miyano, Akira Shigenaga, Minoru Ishikawa, Keita Nakane, Yuya Tanaka, Shinichi Sato, Shusuke Tomoshige, Eri Koyanagi, Hafumi Nishi, Zhengyi Liu
article en
2 citations

Abstract

<h2>Abstract</h2> Our <i>ex situ</i> tyrosine bioconjugation method utilizes the oxidation of <i>N</i>-methylurazole by Bobbitt's salt or electrochemical activation to generate stable radicals for selective tyrosine labeling, thereby addressing the longstanding challenges in protein bioconjugation. Unlike traditional tyrosine conjugation techniques that rely on closed-shell chemistry with 1,2,4-triazoline-3,5-dione derivatives, this method introduces an alternative bond-forming mechanism that expands bioconjugation through a radical-based pathway that enhances tyrosine selectivity. The applicability of this method was demonstrated for various proteins and validated through proteome-wide analyses, highlighting its potential as a valuable tool for investigating protein function and interaction dynamics.

Tetrahedron ChemVol. 12
Otsuka (Japan) (JP), Tohoku University (JP), Ochanomizu University (JP), Fukuyama University (JP), Life Science Institute (JP), Tohoku Medical Megabank Organization (JP), Institute of Science Tokyo (JP), Tokushima University (JP)
Japan Agency for Medical Research and Development
Openalex Percentile: Top 38%
Click Chemistry and Applications
0.50
DOIOpen Access PDFOpenAlex
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