A number of biological processes depend upon the programmed self assembly of biomolecules into higher order self organized systems. The integration of protein-protein self-assembly principles with dendrimer architecture provides a route to novel biomimetic self-assembled systems. We have recently shown that molecules comprising tetravalent leucine-zippers tethered to a core C4 symmetric dendrimer scaffold provides a rational framework for constructing self-assembled supramolecules and fiber-like assemblies that span the nanomolar to micromolar regime [1]. We are currently synthesizing macromolecules that can non-covalently present functional proteins at its periphery. Preliminary results, including synthesis and characterization, will be presented. The ability to rapidly organize naturally expressed proteins on multivalent synthetic scaffolds can potentially impact methods for multivalent targeting of cell-surface receptors.

[1] Zhou, M.; Bentley, D.; Ghosh, I. JACS, 2004, 126, 734-735