Introducing antigen-binding sites in structural loops of immunoglobulin constant domains: Fc fragments with engineered HER2/neu-binding sites and antibody properties.

@article{WozniakKnopp2010IntroducingAS,
  title={Introducing antigen-binding sites in structural loops of immunoglobulin constant domains: Fc fragments with engineered HER2/neu-binding sites and antibody properties.},
  author={Gordana Wozniak-Knopp and Stefan Bartl and Andreas Bauer and Marwa Mostageer and Max Woisetschl{\"a}ger and Bernhard Antes and K Ettl and Manuela Kainer and G Weberhofer and Susanne Wiederkum and Gottfried Himmler and Geert Cornelius Mudde and Florian R{\"u}ker},
  journal={Protein engineering, design & selection : PEDS},
  year={2010},
  volume={23 4},
  pages={289-97}
}
Yeast surface display libraries of human IgG1 Fc regions were prepared in which loop sequences at the C-terminal tip of the CH3 domain were randomized. A high percentage of these library members bound to soluble CD64 and Protein A indicating that the randomization step did not grossly interfere with the overall structure of the displayed Fc. Sorting these libraries by FACS for binders against HER2/neu yielded antigen-specific Fc binders (Fcab; Fc antigen binding) of which one was affinity… CONTINUE READING

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