title: A Self-Assembling Peptide Scaffold for the Multivalent Presentation of Antigens.
abstract: Self-assembling peptides can be used to create tunable higher-order structures for the multivalent presentation of a variety of ligands. We describe a novel, fiber-forming coiled-coil-based peptide that assembles to display, simultaneously, carbohydrate and peptide ligands recognized by biomacromolecules. Preassembly decoration of the scaffold with a diphtheria toxin peptide epitope or a mannose motif did not interfere with self-assembly of the nanostructure. The resulting multivalent display led to tighter binding by antidiphtheria toxin antibodies and mannose-specific carbohydrate binding proteins, respectively. The potential of this self-assembling peptide to display ligands in bioanalytical assays is illustrated by its decoration with a disaccharide glycotope from the Leishmania parasite. Carbohydrate-specific antibodies produced in response to a Leishmania infection are detected more sensitively in human and canine sera due to the multivalent presentation on the self-assembled scaffold. Thus, nanofibers based on coiled-coil peptides are a powerful tool for the development of bioassays and diagnostics.
authors.affiliation: †Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, Germany.
authors.forename: Elsa
authors.initials: E
authors.lastname: Zacco
authors.affiliation: †Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, Germany.|‡Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14424 Potsdam, Germany.
authors.forename: Chakkumkal
authors.initials: C
authors.lastname: Anish
authors.affiliation: †Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, Germany.|‡Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14424 Potsdam, Germany.
authors.forename: Christopher E
authors.initials: CE
authors.lastname: Martin
authors.affiliation: †Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, Germany.|§Research Center of Electron Microscopy and Core Facility BioSupraMol, Institute of Chemistry and Biochemistry, Freie Universität Berlin, Fabeckstraße 36a, 14195 Berlin, Germany.
authors.forename: Hans
authors.initials: H
authors.lastname: V Berlepsch
authors.affiliation: †Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, Germany.
authors.forename: Enrico
authors.initials: E
authors.lastname: Brandenburg
authors.affiliation: †Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, Germany.|‡Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14424 Potsdam, Germany.
authors.forename: Peter H
authors.initials: PH
authors.lastname: Seeberger
authors.affiliation: †Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, Germany.
authors.forename: Beate
authors.initials: B
authors.lastname: Koksch
mesh_terms: D000818:Animals; D017951:Antigen Presentation; D000953:Antigens, Protozoan / Q000378:metabolism; D002241:Carbohydrates / Q000737:chemistry / Q000276:immunology*; D004285:Dogs; D006801:Humans; D007891:Leishmania / Q000276:immunology; D008958:Models, Molecular; D057139:Nanofibers / Q000737:chemistry; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D017433:Protein Structure, Secondary
chemical_list: D000953:Antigens, Protozoan; D002241:Carbohydrates; D010455:Peptides