Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold.
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.
Nygren
Per-Ake
PA
Department of Molecular Biotechnology, School of Biotechnology, Royal Institute of Technology KTH, Stockholm, Sweden. perake@biotech.kth.se
D000818:Animals; D000906:Antibodies / Q000737:chemistry; D001703:Biophysics / Q000379:methods; D002352:Carrier Proteins / Q000737:chemistry*; D020650:Combinatorial Chemistry Techniques / Q000379:methods; D006801:Humans; D008024:Ligands; D009369:Neoplasms / Q000175:diagnosis / Q000628:therapy; D019151:Peptide Library; D011485:Protein Binding; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D000906:Antibodies; D002352:Carrier Proteins; D008024:Ligands; D019151:Peptide Library