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T7 lytic phage-displayed peptide libraries exhibit less sequence bias than M13 filamentous phage-displayed peptide libraries

  1. Author:
    Krumpe, L. R. H.
    Atkinson, A. J.
    Smythers, G. W.
    Kandel, A.
    Schumacher, K. M.
    McMahon, J. B.
    Makowski, L.
    Mori, T.

  2. Author Address

    Takeda Pharmaceut Co Ltd, Biomed Res Labs, Div Pharmaceut Res, Osaka 5328686, Japan. SAIC Frederick Inc, Basic Res Program, Frederick, MD USA. SAIC Frederick Inc, Adv Biomed Comp Ctr, Frederick, MD USA. NCI, Werner H Kirsten Student Internship Program, Ctr Canc Res, Frederick, MD 21701 USA. NCI, Mol Targets Dev Program, Ctr Canc Res, Frederick, MD 21701 USA. Argonne Natl Lab, Argonne, IL 60439 USA.;Mori, T, Takeda Pharmaceut Co Ltd, Biomed Res Labs, Div Pharmaceut Res, 2-17-85 Yodogawa Ku, Osaka 5328686, Japan.;Mori_Toshiyuki2@takeda.co.jp
    1. Year: 2006
    2. Date: Aug
  2. Journal: Proteomics
    1. 6
    2. 15
    3. Pages: 4210-4222
  4. Type of Article: Article
  5. ISSN: 1615-9853
  1. Abstract:

    We investigated whether the T7 system of phage display could produce peptide libraries of greater diversity than the M13 system of phage display due to the differing processes of lytic and filamentous phage morphogenesis. Using a bioinformatics-assisted computational approach, collections of random peptide sequences obtained from a T7 12-mer library (X-12) and a T7 7-mer disulfide-constrained library (CX7C) were analyzed and compared with peptide populations obtained from New England BioLabs' M13 Ph.D.-12 (TM) and Ph.D.-C7C (TM) libraries. Based on this analysis, peptide libraries constructed with the T7 system have fewer amino acid biases, increased peptide diversity, and more normal distributions of peptide net charge and hydropathy than the M13 libraries. The greater diversity of T7-displayed libraries provides a potential resource of novel binding peptides for new as well as previously studied molecular targets. To demonstrate their utility, several of the T7-displayed peptide libraries were screened for streptavidin- and neutravidin-binding phage. Novel binding motifs were identified for each protein.

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External Sources

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  2. DOI: 10.1002/pmic.200500606
  3. View record in Web of Science®
  4. WOS: 000239867600001

Library Notes

  1. Student Author
NCI at Frederick

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