Both in nature and in the laboratory, α-helical coiled coils are formed by the binding of two or more α-helical peptides in a specific manner producing a stable complex in aqueous solution and its stability can be tuned by external parameters like pH, temperature and ions. This versatility arising from a simple helix has resulted in many functions of coiled coils in nature, and has inspired many advances in synthetic biology and supramolecular chemistry. The functions of coiled-coil domains that have been elucidated to date have predominantly been binding, structural and dynamic. It is our long-term goal to understand and harness the emergent properties of complex biological systems. Our approach towards this is the use of biologically inspired modules, for the prescriptive self-assembly of functional synthetic systems<i>. </i>Inspired by examples from nature, we developed coiled coil amphiphiles in order to design (responsive) assemblies with a defined shape and size. Examples on how these assemblies can be used for vaccine applications will be discussed. Furthermore, based on a complementary lipidated coiled coil, we designed a efficient membrane fusion system that is functional in live cells. Initial studies suggest that cargo can be delivered into the cytoplasm of cells by avoiding endosomal pathways, which would revolutionize drug delivery.<br/>

Functional coiled-coil peptides controlled assemblies

249th National Meeting (2015)

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