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Updated: May 7, 2026

Genetic Barcoding with Fluorescent Proteins for Multiplexed Applications
13:14

Genetic Barcoding with Fluorescent Proteins for Multiplexed Applications

Published on: April 14, 2015

A genetically encoded fluorescent amino acid.

Jiangyun Wang1, Jianming Xie, Peter G Schultz

  • 1Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.

Journal of the American Chemical Society
|July 6, 2006
PubMed
Summary
This summary is machine-generated.

Researchers genetically encoded a fluorescent amino acid in E. coli. This novel probe can be used to study protein localization, conformation, and interactions.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Genetically encoded fluorescent amino acids offer powerful tools for studying biological systems.
  • Site-specific incorporation of unnatural amino acids enables detailed investigation of protein function.
  • The amber TAG codon is a widely used system for non-canonical amino acid incorporation.

Purpose of the Study:

  • To genetically encode the fluorescent amino acid l-(7-hydroxycoumarin-4-yl) ethylglycine (1) in E. coli.
  • To evaluate the utility of this novel fluorescent amino acid as a probe in biological systems.

Main Methods:

  • Utilized the amber TAG codon system for site-specific incorporation of the fluorescent amino acid.
  • Grew engineered E. coli strains in the presence of the unnatural amino acid.
  • Characterized the fluorescence properties of the incorporated amino acid.

Main Results:

  • Successfully genetically encoded l-(7-hydroxycoumarin-4-yl) ethylglycine (1) in E. coli.
  • The incorporated amino acid exhibits high fluorescence quantum yield and a large Stoke's shift.
  • The fluorescence is sensitive to environmental factors like pH and polarity.

Conclusions:

  • The genetically encoded fluorescent amino acid l-(7-hydroxycoumarin-4-yl) ethylglycine (1) is a valuable new tool.
  • Its properties make it suitable for probing protein localization, trafficking, conformation, and interactions.