By changing very few positions on the oligomer-forming sequence of a coiled-coil forming peptide, it is possible to obtain an aggregating system for the presentation of ligands in an even more multivalent fashion (Falenski, Bioorg. Med. Chem., 2010). In this SFB 765-funded project, the focus is to optimize the presentation of sugar moieties for their interaction with biological macromolecules (bio-assays will be performed at the Max Plank Institute of Colloids and Interfaces, in collaboration with Dr. Bernd Lepenies; immuno-assays will be performed at the Max Plank Institute of Colloids and Interfaces, in collaboration with Professor Peter Seeberger).
Figure 6. Left, coiled-coil peptide (grey tubes) with spacers (orange lines) and sugars (orange triangles) interacting with three carbohydrate binding domains. Right, self-assembling peptide (spheres) with spacers (lines) and sugars (triangles) presented randomly to the carbohydrate binding domains.