TY - JOUR
T1 - Utilization of single electron transfer reaction in protein chemical labeling
AU - Sato, Shinichi
AU - Tsushima, Michihiko
AU - Nakamura, Hiroyuki
N1 - Publisher Copyright:
© 2019 Society of Synthetic Organic Chemistry. All rights reserved.
PY - 2019
Y1 - 2019
N2 - The chemical labeling of proteins with synthetic small compound is an important technique in chemical biology. To achieve reliable bioconjugation. rapid reactions in aqueous under physiological pH and mild temperature are required. In the attempt to covalently label native proteins, various biorthogonal chemical reactions targeting not only nucleophilic amino acid residues such as lysine and cysteine, but also tyrosine, tryptophan, methionine, N-and C-terminal positions have been developed. The radical protein labeling reaction proceeds rapidly even in intracellular and physiological environment, and high reactivity of radical species enables local reaction control on the nanometer scale. In this paper, we introduce our recent studies on the labeling of protein tyrosine residues via single electron transfer initiated radical reaction, especially using ruthenium photocatalyst. We found the protein labeling at tyrosine residues with small compounds such as N-acyl-N,N-phenylenediamine and l-methyl-4-aryl-urazole under the reaction condition using ruthenium photocatalyst and visible light irradiation. Target-selective labeling using ligand-conju-gated ruthenium photocatalysts, and target-selective-purification and labeling from protein mixture using catalyst-functionalized affinity beads were achieved.
AB - The chemical labeling of proteins with synthetic small compound is an important technique in chemical biology. To achieve reliable bioconjugation. rapid reactions in aqueous under physiological pH and mild temperature are required. In the attempt to covalently label native proteins, various biorthogonal chemical reactions targeting not only nucleophilic amino acid residues such as lysine and cysteine, but also tyrosine, tryptophan, methionine, N-and C-terminal positions have been developed. The radical protein labeling reaction proceeds rapidly even in intracellular and physiological environment, and high reactivity of radical species enables local reaction control on the nanometer scale. In this paper, we introduce our recent studies on the labeling of protein tyrosine residues via single electron transfer initiated radical reaction, especially using ruthenium photocatalyst. We found the protein labeling at tyrosine residues with small compounds such as N-acyl-N,N-phenylenediamine and l-methyl-4-aryl-urazole under the reaction condition using ruthenium photocatalyst and visible light irradiation. Target-selective labeling using ligand-conju-gated ruthenium photocatalysts, and target-selective-purification and labeling from protein mixture using catalyst-functionalized affinity beads were achieved.
KW - Affinity beads
KW - Protein labeling
KW - Proximity labeling
KW - Ruthenium photocatalyst
KW - Single electron transfer
KW - Tyrosine labeling
UR - http://www.scopus.com/inward/record.url?scp=85065983140&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85065983140&partnerID=8YFLogxK
U2 - 10.5059/yukigoseikyokaishi.77.463
DO - 10.5059/yukigoseikyokaishi.77.463
M3 - Article
AN - SCOPUS:85065983140
VL - 77
SP - 463
EP - 471
JO - Yuki Gosei Kagaku Kyokaishi/Journal of Synthetic Organic Chemistry
JF - Yuki Gosei Kagaku Kyokaishi/Journal of Synthetic Organic Chemistry
SN - 0037-9980
IS - 5
ER -