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Libraries phage-displayed

Biologic library Phage-display Provides up to 10 peptide entities Limited to peptide libraries with... [Pg.1427]

G. P. Smith described in a seminal paper the use of filamentous phage for the synthesis of peptide libraries (phage display method. Science, 1985,228, 1315)... [Pg.6]

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,... 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... [Pg.364]

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. [Pg.365]

Dennis, M.S., Lazarus, R.A. Kunitz domain inhibitors of tissue factor-factor Vila. 1. Potent inhibitors selected from libraries by phage display. /. Biol. Chem. 269 22129-22136, 1994. [Pg.372]

The advantage of the Jun-Fos phage display system is that the fusion of the library DNA is to the C-terminus of a protein rather than between the... [Pg.63]

Cochrane, D., Webster, C., Masih, G., and McCafferty, J. (2000). Identification of natural ligands for SH2 domains from a phage display cDNA library. J. Mol. Biol. 297, 89-97. [Pg.112]

Palzkill, T., Huang, W., and Weinstock, G. M. (1998). Mapping protein-ligand interactions using whole genome phage display libraries. Gene 221, 79-83. [Pg.119]

Pasqualini, R., and Ruoslahti, E. (1996). Organ targeting in vivo using phage display peptide libraries. Nature 380, 364-366. [Pg.119]

Rader, C., and Barbas, C. F., Ill (1997). Phage display of combinatorial antibody libraries. Curr. Opin. Biotechnol. 8, 503-508. [Pg.120]

Vaughan, T. J., Williams, A. J., Pritchard, K., Osbourn, J. K., Pope, A. R., Eamshaw, J. C., McCafferty, J., Hodits, R. A., Wilton, J., and Johnson, K. S. (1996). Human antibodies with sub-nanomolar affinities isolated from a large non-immunized phage display library. Nat. Biotechnol. 14, 309-314. [Pg.123]

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. [Pg.124]

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-... [Pg.527]


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See also in sourсe #XX -- [ Pg.67 , Pg.68 , Pg.69 , Pg.71 , Pg.73 , Pg.75 , Pg.76 , Pg.81 ]




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Combinatorial peptide library phage display

Constrained phage-displayed peptide librarie

Phage

Phage display

Phage display antibody library

Phage display libraries, antibody evolution

Phage display libraries, construction

Phage display library

Phage display library

Phage display library design, construction

Phage libraries

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