Anticalins are artificial proteins that are able to bind to antigens, either to proteins or to small molecules. They are not structurally related to antibodies, which makes them a type of antibody mimetic. Instead, they are derived from human lipocalins which are a family of naturally binding proteins. Anticalins are being used in lieu of monoclonal antibodies, but are about eight times smaller with a size of about 180 amino acids and a mass of about 20 kDa.
They were mainly developed at the University of Technology Munich and are currently used as research tools. Diagnostic and therapeutic applications, including the use for targeted drug delivery, are being aimed at. The underlying technology was nominated for the German Future Prize in 2004.
Characteristic for anticalins is their barrel structure formed by eight antiparallel β-strands pairwise connected by loops and an attached α-helix. The main structure of anticalins is identical to wild type lipocalins. Conformational deviations are primarily located in the four loops reaching in the ligand binding site. Mutagenesis of amino acids at the binding site allows for changing the affinity and selectivity.
- Skerra A (June 2008). "Alternative binding proteins: anticalins - harnessing the structural plasticity of the lipocalin ligand pocket to engineer novel binding activities". FEBS J. 275 (11): 2677–83. doi:10.1111/j.1742-4658.2008.06439.x. PMID 18435758.
- Mutschler, Ernst; Schäfer-Korting, Monika (2001). Arzneimittelwirkungen (in German) (8 ed.). Stuttgart: Wissenschaftliche Verlagsgesellschaft. p. 911. ISBN 3-8047-1763-2.
- Skerra, A (2002). "Anticaline". BIOforum (in German) (Darmstadt: GIT Verlag). 4/2002: 227–229.
- "Deutscher Zukunftspreis 2004: Anticaline – Biopharmazeutische Wirkstoffe durch Protein-Design" [German Future Prize 2004: Anticalins – Biopharmaceutical agents by protein design] (in German). Stifterverband für die Deutsche Wissenschaft. Retrieved 6 December 2010.