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Single domain protein scaffold
Single domain protein scaffold












single domain protein scaffold

"Engineering a targeted delivery platform using Centyrins".

  • ^ Goldberg SD, Cardoso RM, Lin T, Spinka-Doms T, Klein D, Jacobs SA, et al.
  • "Monobodies as possible next-generation protein therapeutics - a perspective".
  • ^ "Rapid identification and development of SARS-CoV-2 selective Optimers".
  • "Development of polyol-responsive antibody mimetics for single-step protein purification".
  • ^ Suderman RJ, Rice DA, Gibson SD, Strick EJ, Chao DM (April 17, 2017).
  • "Monobodies: antibody mimics based on the scaffold of the fibronectin type III domain".

    single domain protein scaffold

    "Engineered protein inhibitors of proteases". "Gastrobodies are engineered antibody mimetics resilient to pepsin and hydrochloric acid". ^ Wicke N, Bedford MR, Howarth M (August 2021)."A novel, non-immunogenic Fyn SH3-derived binding protein with tumor vascular targeting properties". ^ Grabulovski D, Kaspar M, Neri D (February 2007)."DARPins: a new generation of protein therapeutics". ^ Stumpp MT, Binz HK, Amstutz P (August 2008)."Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains". "Alternative binding proteins: anticalins - harnessing the structural plasticity of the lipocalin ligand pocket to engineer novel binding activities". Developing a small, simple protein domain that includes a similar sized binding region to antibody complementarity determining regions (CDRs) is a successful strategy for overcoming the complexity of antibody structure. "Structural basis of IL-23 antagonism by an Alphabody protein scaffold". ^ Desmet J, Verstraete K, Bloch Y, Lorent E, Wen Y, Devreese B, et al."Artificial binding proteins (Affitins) as probes for conformational changes in secretin PulD". ^ Krehenbrink M, Chami M, Guilvout I, Alzari PM, Pécorari F, Pugsley AP (November 2008)."Sensitive Affimer and antibody based impedimetric label-free assays for C-reactive protein". ^ Johnson A, Song Q, Ko Ferrigno P, Bueno PR, Davis JJ (Aug 7, 2012)."Affilin-novel binding molecules based on human gamma-B-crystallin, an all beta-sheet protein". ^ Ebersbach H, Fiedler E, Scheuermann T, et al."Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold". "Engineered protein scaffolds as next-generation antibody therapeutics". Highly stable fibronectin type III (FN3) domainĪ high affinity binding protein domain engineered to bind to Hen Egg-white Lysozyme

    single domain protein scaffold

    Kunitz domains of various protease inhibitorsĬarbohydrate Binding Module 32-2 (from Clostridium perfringens NagH)įlexible nucleic acid based scaffold G-quadruplexįourteenth fibronectin type-III scaffold of Human Fibronectin (14Fn3) Antibody mimetics are being developed as therapeutic and diagnostic agents. Nucleic acids and small molecules are sometimes considered antibody mimetics as well, but not artificial antibodies, antibody fragments and fusion proteins composed from these.Ĭommon advantages over antibodies are better solubility, tissue penetration, stability towards heat and enzymes, and comparatively low production costs. They are usually artificial peptides or proteins with a molar mass of about 3 to 20 kDa. Institute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.Antibody mimetics are organic compounds that, like antibodies, can specifically bind antigens, but that are not structurally related to antibodies. The procedure yielded scaffold-related variants with nanomolar affinity. We demonstrated its functionality by training it as a binder against human interleukin-10, a medically important cytokine. The newly developed scaffold, called ProBi (Protein Binder), contains two independently mutable surface patches. We proved the applicability of this systematic procedure by selecting a monomeric single-domain human protein with a fold different from previously known scaffolds. In the next step, we examined several variants of the candidate scaffolds including their wild types and alanine mutants. The candidate protein scaffolds were subjected to a thorough screening including computational evaluation of the mutability, and experimental determination of their expression yield in E. We hereby describe a process based on an analysis of protein structures from the Protein Data Bank and their experimental examination. This calls for a more systematic approach in designing new scaffolds suitable for use in one or more methods of directed evolution. The advantages include smaller size and a more robust, single-domain structural framework with a defined binding surface amenable to mutation. Diversity, Equity, Inclusion, and AccessĮngineered small non-antibody protein scaffolds are a promising alternative to antibodies and are especially attractive for use in protein therapeutics and diagnostics.Citation, Usage, Privacy Policies, Logo.Biologically Interesting Molecule Reference Dictionary (BIRD).














    Single domain protein scaffold