Abstract
Affilin® molecules represent a new class of so-called scaffold proteins. The concept of scaffold proteins is to use stable and versatile protein structures which can be endowed with de novo binding properties and specificities by introducing mutations in surface exposed amino acid residues. Complex variations and combinations are generated by genetic methods of randomization resulting in large cDNA libraries. The selection for candidates binding to a desired target can be executed by display methods, especially the very robust and flexible phage display. Here, we describe the construction of ubiquitin based Affilin® phage display libraries and their use in biopanning experiments for the identification of novel protein ligands.
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Acknowledgment
We thank Anja Kunert for early work on the protocols, Ulrich Haupts for helpful discussions, and Erik Fiedler for chromatographic purification of the phage libraries.
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Settele, F., Zwarg, M., Fiedler, S., Koscheinz, D., Bosse-Doenecke, E. (2018). Construction and Selection of Affilin® Phage Display Libraries. In: Hust, M., Lim, T. (eds) Phage Display. Methods in Molecular Biology, vol 1701. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7447-4_11
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DOI: https://doi.org/10.1007/978-1-4939-7447-4_11
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