Phage display peptides

DeLeo FR, Yu L, Burritt JB, Bond CW, Jesaitis AJ, Quinn MT, Mapping sites of interaction of p47-phox and flavocytochrome b with random-sequence peptide phage display libraries, Proc. Natl. Acad. Sci. USA, 92 7110-7114, 1995. 

Samoylova TI, Morrison NE, Globa LP, Cox NR. Peptide phage display opportunities for development of personaUzed anti-cancer strategies. Anti-Cancer Agents Med. Chem. 2006 6 9-17. 

Random peptide phage display library such as fUSE5 or f88-4 (From George P. Smith, Department of Biological Sciences, University of Missouri, Columbia). 

Amplified and purified precleared random peptide phage display library (see Subheading 2.4). 

Zhang, J., Spring, H., and Schwab, M. (2001) Neuroblastoma tumor cell-binding peptides identified through random peptide phage display. Cancer Lett. 171, 153-164... 

M.A. Myers, et al., (2000). Conformational epitopes on the diabetes autoantigen GAD65 identified by peptide phage display and molecular modeling. J. Immunol. 165, 3830-3838. 

Figure 17.10 Construction of a two helix truncated Z domain, (a) Diagram of the three-helix bundle Z domain of protein A (blue) bound to the Fc fragment of IgG (green). The third helix stabilizes the two Fc-binding helices, (b) Three phage-display libraries of the truncated Z-domaln peptide were selected for binding to the Fc. First, four residues at the former helix 3 interface ("exoface") were sorted the consensus sequence from this library was used as the template for an "intrafece" library, in which residues between helices 1 and 2 were randomized. The most active sequence from this library was used as a template for five libraries in which residues on the Fc-binding face ("interface") were randomized. Colored residues were randomized blue residues were conserved as the wild-type amino acid while yellow residues reached a nonwild-type consensus, [(b) Adapted from A.C. Braisted and J.A. Wells,...

Phage display of random peptide libraries identified agonists of erythropoietin receptor... 

EMPl, selected by phage display from random peptide libraries, demonstrates that a dimer of a 20-residue peptide can mimic the function of a monomeric 166-residue protein. In contrast to the minimized Z domain, this selected peptide shares neither the sequence nor the structure of the natural hormone. Thus, there can be a number of ways to solve a molecular recognition problem, and combinatorial methods such as phage display allow us to sort through a multitude of structural scaffolds to discover novel solutions. 

Kay, B.K, Winter, J., McCafferty, J. eds. Phage Display of Peptides and Proteins a Laboratory Manual. San Diego Academic Press, 1996. 

Structural scaffolds can be reduced in size while function is retained Phage display of random peptide librciries... 

Pasqualini, R., and Ruoslahti, E. (1996). Organ targeting in vivo using phage display peptide libraries. Nature 380, 364-366. 

Yao, Z.-J., Kao, M. C. C., and Chung, M. C. M. (1995). Epitope identification by polyclonal antibody from phage-displayed random peptide library. J. Protein Chem. 14, 161-166. 

We have previously developed an in vivo selection method in which peptides that home to specific vascular beds are selected after intravenous administration of a phage display random peptide library [5]. This strategy revealed a vascular address system that allows tissue-specific targeting of normal blood vessels [6-8] and angiogenesis-related targeting of tumor blood vessels [3, 6, 9-12]. While the biologi-... 

Rajotte D, Ruoslahti E. Membrane dipeptidase is the receptor for a lung-targeting peptide identified by in vivo phage display. J Biol Chem 1999 274 11593-11598. 

Chen, I., Choi, Y. A. and Ting, A. Y. (2007). Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins. J. Am. Chem. Soc. 129, 6619-25. 

Naik, R.R., Brott, L.L., Clarson, S.J. and, Stone, M.O. (2002) Silica-precipitating peptides isolated from a combinatorial phage display peptide library. Journal of Nanoscience and Nanotechnology, 2, 95-100. 

Sompuram SR, Kodela V, Ramanathan H, et al. Synthetic peptides identified from phage-displayed combinatorial libraries as immunodiagnostic assay surrogate quality-control targets. Clin. Chem. 2002 48 410-420. 

Figure 16.4 Graph depicting the percentage of lysine residues among peptides that bind to the indicated monoclonal antibodies. The peptides were isolated after affinity selection (biopanning) from a phage-displayed combinatorial peptide library. The peptides are grouped as to whether they are susceptible to formalin fixation, resulting in a loss of immunoreactivity.

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