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Phage Display Technology

Affinity Selection by Biopanning

  • Protocol
Affinity Chromatography

Part of the book series: Methods in Molecular Biology ((MIMB,volume 147))

Abstract

Phage display technology (1) is rapidly evolving as a biomolecular tool with applications in the discovery of ligands for affinity chromatography and drugs (2,3), in the study of protein/protein interactions (4), and in epitope mapping (5,6), among others. This technology relies on the utilization of phage display libraries (see Notes 1 and 2) in a screening process known as biopanning (7).

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References

  1. Smith G. P. (1985) Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228, 1315–1317.

    Article  PubMed  CAS  Google Scholar 

  2. Maclennan J., Ransohoff T., Potter D., and Oleksyszyn J. (1997) The generation of process suitable, rugged, targeted affinity ligands using phage display technology. Twelfth International Symposium on Affinity Interactions: Fundamentals and Applications of Biomolecular Recognition. Kalmar, Sweden. Abstract L30.

    Google Scholar 

  3. Doorbar J. and Winter G. (1994) Isolation of a peptide antagonist to the thrombin receptor using phage display. J. Mol. Biol. 244, 361–369.

    Article  PubMed  CAS  Google Scholar 

  4. Hong S. S. and Boulanger P. (1995) Protein ligands of the human adenovirus type 2 outer capsid identified by biopanning of a phage-displayed peptide library on separate domains of wild-type and mutant penton capsomers. EMBO J. 14, 4714–4727.

    PubMed  CAS  Google Scholar 

  5. Cwirla S. E., Peters E. A., Barrett R. W., and Dower W. J. (1990) Peptides on phage: a vast library of peptides for identifying ligands. Proc. Natl. Acad. Sci. USA 87, 6378–6382.

    Article  PubMed  CAS  Google Scholar 

  6. Scott J. K. and Smith G. P. (1990) Searching for peptide ligands with an epitope library. Science 249, 386–390.

    Article  PubMed  CAS  Google Scholar 

  7. Smith G. P. and Scott J. K. (1993) Libraries of peptides and proteins displayed on filamentous phage. Methods Enzymol. 217, 228–257.

    Article  PubMed  CAS  Google Scholar 

  8. Sambrook J., Fritsch E., and Maniatis T. (eds.) (1989) Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, PC24.

    Google Scholar 

  9. Ehrlich G. K., Andria M. L., Zheng X., Kieffer B., Gioannini T. L., Hiller J. M., Rosenkranz J. E., Veksler B. M., Zukin R. S., and Simon E. J. (1998) Functional significance of cysteine residues in the delta opioid receptor studied by sitedirected mutagenesis. Can. J. Physiol. Pharmocol. 76, 269–277.

    Article  CAS  Google Scholar 

  10. Goodson R. J., Doyle M. V., Kaufman S. E., and Rosenberg S. (1994) Highaffinity urokinase receptor antagonists identified with bacteriophage peptide display. Proc. Natl. Acad. Sci. USA 91, 7129–7133.

    Article  PubMed  CAS  Google Scholar 

  11. Szardenings M., Tornroth S., Mutulis F., Muceniece R., Keinanen K., Kuusinen A., and Wikberg J. E. S. (1997) Phage display selection on whole cells yields a peptide specific for melanocortin receptor 1. J. Biol. Chem., 272, 27,943–27,948.

    Article  PubMed  CAS  Google Scholar 

  12. Hammer J., Takacs B., and Sinigaglia F. (1992) Identification of a motif for HLADR1 binding peptides using M13 display libraries. J. Exp. Med. 176, 1007–1013.

    Article  PubMed  CAS  Google Scholar 

  13. Glaser V. (1997) Conflicts brewing as phage display gets complex. Nature Biotechnol. 15, 506.

    Article  CAS  Google Scholar 

  14. Cabilly S., Heldman J., Heldman E., and Katchalski-Katzir E. (1998) The use of combinatorial libraries to identify ligands that interact with surface receptors in living cells, in Methods in Molecular Biology, vol. 87: Combinatorial Peptide Library Protocols (Cabilly S., ed.), Humana Press, Totowa, NJ, 175–183.

    Google Scholar 

  15. Giebel L. B., Cass R. T., Milligan D. L., Young D. C., Arze R., and Johnson C. R. (1995) Screening of cyclic peptide phage libraries identifies ligands that bind streptavidin with high affinity. Biochemistry 34, 15,430–15,435.

    Article  PubMed  CAS  Google Scholar 

  16. Adey N. B., Mataragnon A. H., Rider J. E., Carter J. M., and Kay B. K. (1995) Characterization of phage that bind plastic from phage-displayed random peptide libraries. Gene 156, 27–31.

    Article  PubMed  CAS  Google Scholar 

  17. Spada S. Krebber C., and Pluckthun A. (1997) Selectively infective phages (SIP). Biol. Chem. 378, 445–456.

    Article  PubMed  CAS  Google Scholar 

  18. Sparks A. B., Adey N. B., Cwirla S., and Kay B. K. (1996) Screening phagedisplayed random peptide libraries, in Phage Display of Peptides and Proteins (Kay B. K., Winter J., and McCafferty J., eds.), Academic, San Diego, CA, 227–253.

    Chapter  Google Scholar 

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Ehrlich, G.K., Berthold, W., Bailon, P. (2000). Phage Display Technology. In: Bailon, P., Ehrlich, G.K., Fung, WJ., Berthold, W. (eds) Affinity Chromatography. Methods in Molecular Biology, vol 147. Humana Press. https://doi.org/10.1007/978-1-60327-261-2_18

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  • DOI: https://doi.org/10.1007/978-1-60327-261-2_18

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-694-9

  • Online ISBN: 978-1-60327-261-2

  • eBook Packages: Springer Protocols

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