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2012 | 59 | 3 | 383-390
Article title

A novel, stable, helical scaffold as an alternative binder - construction of phage display libraries

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Abstracts
EN
Specific, high affinity binding macromolecules are of great importance for biomedical and biotechnological applications. The most popular classical antibody-based molecules have recently been challenged by alternative scaffolds with desirable biophysical properties. Phage display technology applied to such scaffolds allows generation of potent affinity reagents by in vitro selection. Here, we report identification and characterization of a novel helical polypeptide with advantageous biophysical properties as a template for construction of phage display libraries. A three-helix bundle structure, based on Measles virus phosphoprotein P shows a very favourable stability and solubility profile. We designed, constructed and characterized six different types of phage display libraries based on the proposed template. Their functional size of over 109 independent clones, balanced codon bias and decent display level are key parameters attesting to the quality and utility of the libraries. The new libraries are a promising tool for isolation of high affinity binders based on a small helical scaffold which could become a convenient alternative to antibodies.
Publisher

Year
Volume
59
Issue
3
Pages
383-390
Physical description
Dates
published
2012
received
2012-03-26
revised
2012-06-25
accepted
2012-08-20
(unknown)
2012-09-18
Contributors
  • Department of Protein Engineering, Faculty of Biotechnology, University of Wroclaw, Wrocław, Poland
  • Department of Protein Engineering, Faculty of Biotechnology, University of Wroclaw, Wrocław, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv59p383kz
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