Phage Wrapping with Cationic Polymers Eliminates Nonspecific Binding between M13 Phage and High pI Target Proteins
| Autor: | Zhibin Guan, Gregory A. Weiss, Edmund F. Palermo, Kristeene A. Knopp, Denise Der, Ozgul Tezgel, Kenichi Kuroda, Hiromitsu Urakami, Gregory N. Tew, Cathie M. Overstreet, Ting Bin Yu, Jorge A. Lamboy, Jessica A. Arter |
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| Rok vydání: | 2009 |
| Předmět: |
Phage display
Polymers Surface Properties viruses Phagemid Molecular Conformation Biochemistry Article Catalysis Substrate Specificity Colloid and Surface Chemistry Cations Pi Binding site chemistry.chemical_classification Nonspecific binding Binding Sites Chemistry Cationic polymerization Proteins General Chemistry Polymer Hydrogen-Ion Concentration Combinatorial chemistry Solubility Biophysics Target protein Bacteriophage M13 |
| Zdroj: | Journal of the American Chemical Society. 131:16454-16460 |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/ja9050873 |
| Popis: | M13 phage have provided scaffolds for nanostructure synthesis based upon self-assembled inorganic and hard materials interacting with phage-displayed peptides. Additionally, phage display has been used to identify binders to plastic, TiO2, and other surfaces. However, synthesis of phage-based materials through the hybridization of soft materials with the phage surface remains unexplored. Here, we present an efficient “phage wrapping” strategy for the facile synthesis of phage coated with soluble, cationic polymers. Polymers bearing high positive charge densities demonstrated the most effective phage wrapping, as shown by assays for blocking non-specific binding of the anionic phage coat to a high pI target protein. The results establish the functional group requirements for hybridizing phage with soft materials, and solve a major problem in phage display – non-specific binding by the phage to high pI target proteins. |
| Databáze: | OpenAIRE |
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