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Trinucleotide cassettes increase diversity of T7 phage-displayed peptide library

  1. Author:
    Krumpe, L. R.
    Schumacher, K. M.
    McMahon, J. B.
    Makowski, L.
    Mori, T.

  2. Author Address

    [Krumpe, Lauren Rh; Schumacher, Kathryn M.; McMahon, James B.; Mori, Toshiyuki] NCI, Canc Res Ctr, Mol Targets Dev Program, Frederick, MD 21702 USA. [Krumpe, Lauren Rh] NCI, SAIC Frederick Inc, Frederick, MD 21702 USA. [Schumacher, Kathryn M.] NCI, Werner H Kirsten Student Internship Program, Frederick, MD 21702 USA. [Makowski, Lee] Argonne Natl Lab, Biosci Div, Argonne, IL 60439 USA.;Mori, T (reprint author), NCI, Canc Res Ctr, Mol Targets Dev Program, Frederick, MD 21702 USA.;lhaugh@ncifcrf.gov; kschu@mit.edu; mcmahon@ncifcrf.gov; imakowski@anl.gov; Mori_Toshiyuki2@takeda.co.jp
    1. Year: 2007
    2. Date: Oct
  2. Journal: BMC Biotechnology
    1. 7
  4. Type of Article: Article
  5. Article Number: 65
  6. ISSN: 1472-6750
  1. Abstract:

    Background: Amino acid sequence diversity is introduced into a phage-displayed peptide library by randomizing library oligonucleotide DNA. We recently evaluated the diversity of peptide libraries displayed on T7 lytic phage and M13 filamentous phage and showed that T7 phage can display a more diverse amino acid sequence repertoire due to differing processes of viral morphogenesis. Methods: In this study, we evaluated and compared the diversity of a 12-mer T7 phage-displayed peptide library randomized using codon-corrected trinucleotide cassettes with a T7 and an M13 12-mer phage-displayed peptide library constructed using the degenerate codon randomization method. Conclusion: The combination of T7 phage display and trinucleotide cassette randomization resulted in a novel resource for the potential isolation of binding peptides for new and previously studied molecular targets.

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External Sources

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  2. DOI: 10.1186/1472-6750-7-65
  3. PMID: 17919322
  4. View record in Web of Science®
  5. WOS: 000252448500001

Library Notes

  1. Student Author
NCI at Frederick

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