A Self-Assembling Peptide Scaffold for the Multivalent Presentation of Antigens

E. Zacco, C. Anish, C. E. Martin, H. v. Berlepsch, E. Brandenburg, P. H. Seeberger, B. Koksch – 2015

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.

Titel
A Self-Assembling Peptide Scaffold for the Multivalent Presentation of Antigens
Verfasser
E. Zacco, C. Anish, C. E. Martin, H. v. Berlepsch, E. Brandenburg, P. H. Seeberger, B. Koksch
Datum
2015
Kennung
10.1021/acs.biomac.5b00572
Zitierweise
Biomacromolecules, 2015, 16 (7), 2188–2197
Art
Text
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