Fluorogenic protein labeling using a genetically encoded unstrained alkene

X. Shang, X. Song, C. Faller, Rebecca Y Lai, Hui Li, Ronald Cerny, Wei Niu, Jiantao Guo

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

We developed a new fluorogenic bioorthogonal reaction that is based on the inverse electron-demand Diels-Alder reaction between styrene (an unstrained alkene) and a simple tetrazine. The reaction forms a new fluorophore with no literature precedent. We have identified an aminoacyl-tRNA synthetase/tRNA pair for the efficient and site-specific incorporation of a styrene-containing amino acid into proteins in response to amber nonsense codon. Fluorogenic labeling of purified proteins and intact proteins in live cells were demonstrated. The fluorogenicity of the styrene-tetrazine reaction can be potentially applied to the study of protein folding and function under physiological conditions with low background fluorescence interference.

Original languageEnglish (US)
Pages (from-to)1141-1145
Number of pages5
JournalChemical Science
Volume8
Issue number2
DOIs
StatePublished - Jan 1 2017

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Styrene
Alkenes
Labeling
Amber
Protein folding
Amino Acyl-tRNA Synthetases
Proteins
Fluorophores
Transfer RNA
Fluorescence
Amino Acids
Electrons

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Fluorogenic protein labeling using a genetically encoded unstrained alkene. / Shang, X.; Song, X.; Faller, C.; Lai, Rebecca Y; Li, Hui; Cerny, Ronald; Niu, Wei; Guo, Jiantao.

In: Chemical Science, Vol. 8, No. 2, 01.01.2017, p. 1141-1145.

Research output: Contribution to journalArticle

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