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Alternative binding proteins: Affibody binding proteins developed from a small three-helix bundle scaffold
KTH, School of Biotechnology (BIO), Molecular Biotechnology.ORCID iD: 0000-0003-4214-6991
2008 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 275, no 11, 2668-2676 p.Article, review/survey (Refereed) Published
Abstract [en]

In recent years, classical antibody-based affinity reagents have been challenged by novel types of binding proteins developed by combinatorial protein engineering principles. One of these classes of binding proteins of non-Ig origin are the so-called affibody binding proteins, functionally selected from libraries of a small (6 kDa), non-cysteine three-helix bundle domain used as a scaffold. During the first 10 years since they were first described, high-affinity affibody binding proteins have been selected towards a large number of targets for use in a variety of applications, such as bioseparation, diagnostics, functional inhibition, viral targeting and in vivo tumor imaging/therapy. The small size offers the possibility to produce functional affibody binding proteins also by chemical synthesis production routes, which has been found to be advantageous for the site-specific introduction of various labels and radionuclide chelators.

Place, publisher, year, edition, pages
2008. Vol. 275, no 11, 2668-2676 p.
Keyword [en]
affibody binding proteins, affinity chromatography, combinatorial, protein engineering, in vivo imaging, peptide synthesis, phage display, protein chips, protein-protein interactions, selection, viral, retargeting, staphylococcal surface display, bacterial receptor domain, growth-factor receptor, taq dna-polymerase, combinatorial libraries, escherichia-coli, fluorescent detection, capture microarrays, structural basis, molecules
URN: urn:nbn:se:kth:diva-17529DOI: 10.1111/j.1742-4658.2008.06438.xISI: 000255822000002ScopusID: 2-s2.0-43549101411OAI: diva2:335573
QC 20100525Available from: 2010-08-05 Created: 2010-08-05Bibliographically approved

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Nygren, Per-Åke
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