Biological assemblies therefore share properties with synthetic materials denoted “soft matter”, i.e. they are fluctuating, susceptible to external fields and follow the same physics as synthetic analogs such as surfactants, polymers and colloids. While regular synthetic amphiphiles readily form well-defined (e.g. spherical, cylindrical) nanostructures, they lack the structural specificity and encoded biological function found for proteins, which consist of well-defined amino acid sequences.

The potential of mimicking natural protein-based materials and control their function using fully synthetic materials is strongly appealing for many biomedical and nanotechnological applications. The current bottleneck in this field is not necessarily synthetic methods; the recent decade has seen a significant development in synthesis of hybrid systems involving biological building blocks such as peptides, proteins and lipids, or peptidomimetics such as peptoids (poly-N-substituted glycines).  For a full application of such systems, the design rules for both spontaneous and guided formation must be known. This requires fundamental insight into their thermodynamics, kinetic pathways of formation, dynamics and response towards external perturbation.

• PhD student Nico König
• Post Doc Matthias Amann

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