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Protein evolution with an expanded genetic code

Academic Article
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Overview

related to degree

  • Mills, Jeremy, Ph.D. in Chemistry, Scripps Research 2002 - 2010
  • Lee, Hyun Soo, Ph.D. in Chemistry, Scripps Research 2005 - 2009
  • Liu, Chang Chun, Ph.D. in Chemistry, Scripps Research 2005 - 2009

authors

  • Liu, Chang Chun
  • Mack, A. V.
  • Tsao, M. L.
  • Mills, Jeremy
  • Lee, Hyun Soo
  • Choe, Hyeryun
  • Farzan, Michael
  • Schultz, Peter
  • Smider, Vaughn

publication date

  • November 2008

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • We have devised a phage display system in which an expanded genetic code is available for directed evolution. This system allows selection to yield proteins containing unnatural amino acids should such sequences functionally outperform ones containing only the 20 canonical amino acids. We have optimized this system for use with several unnatural amino acids and provide a demonstration of its utility through the selection of anti-gp120 antibodies. One such phage-displayed antibody, selected from a na?ve germline scFv antibody library in which six residues in V(H) CDR3 were randomized, contains sulfotyrosine and binds gp120 more effectively than a similarly displayed known sulfated antibody isolated from human serum. These experiments suggest that an expanded "synthetic" genetic code can confer a selective advantage in the directed evolution of proteins with specific properties.
  • We have devised a phage display system in which an expanded genetic code is available for directed evolution. This system allows selection to yield proteins containing unnatural amino acids should such sequences functionally outperform ones containing only the 20 canonical amino acids. We have optimized this system for use with several unnatural amino acids and provide a demonstration of its utility through the selection of anti-gp120 antibodies. One such phage-displayed antibody, selected from a naïve germline scFv antibody library in which six residues in V(H) CDR3 were randomized, contains sulfotyrosine and binds gp120 more effectively than a similarly displayed known sulfated antibody isolated from human serum. These experiments suggest that an expanded "synthetic" genetic code can confer a selective advantage in the directed evolution of proteins with specific properties.

subject areas

  • Amino Acids
  • Antibodies, Viral
  • Directed Molecular Evolution
  • Enzyme-Linked Immunosorbent Assay
  • Escherichia coli
  • Genetic Code
  • Genetic Vectors
  • Germ Cells
  • HIV
  • HIV Envelope Protein gp120
  • Humans
  • Peptide Library
  • Proteins
  • Sequence Analysis, Protein
  • Tyrosine
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Research

keywords

  • directed evolution
  • phage display
  • unnatural amino acids
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Identity

PubMed Central ID

  • PMC2584696

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0809543105

PubMed ID

  • 19004806
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Additional Document Info

start page

  • 17688

end page

  • 17693

volume

  • 105

issue

  • 46

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