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Encoding Noncanonical Amino Acids into Phage Displayed Proteins.

Cristina Díaz-Perlas1, Montserrat Escobar-Rosales1, Charles W Morgan2

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This study integrates phage display with genetic code expansion to incorporate noncanonical amino acids (ncAAs) into antibodies. This advances protein engineering for novel applications in imaging and materials science.

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Bioorthogonal reactionsCyclopropenePhage displayProtein engineeringSite-specific bioconjugation

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Area of Science:

  • Biotechnology
  • Protein Engineering
  • Synthetic Biology

Background:

  • Phage display is a powerful technique for evolving proteins but is limited by naturally encoded amino acids.
  • Genetic code expansion offers a method to incorporate noncanonical amino acids (ncAAs) into proteins.

Purpose of the Study:

  • To describe a method for incorporating one or two ncAAs into single-chain fragment variable (scFv) antibodies using phage display.
  • To expand the chemical diversity of phage-displayed proteins.

Main Methods:

  • Utilized amber or quadruplet codons to direct the incorporation of ncAAs.
  • Employed a pyrrolysyl-tRNA synthetase/tRNA pair for lysine derivative incorporation.
  • Employed an orthogonal tyrosyl-tRNA synthetase/tRNA pair for phenylalanine derivative incorporation.

Main Results:

  • Successfully incorporated one or two ncAAs into scFv antibodies displayed on phage.
  • Demonstrated the feasibility of expanding the chemical repertoire of phage-displayed proteins.

Conclusions:

  • The described method enables the creation of phage-displayed proteins with novel chemical functionalities.
  • This approach lays the groundwork for advanced applications in imaging, targeted delivery, and novel material development.