Investigation of the structural symmetry of homomeric coiled-coil peptides using BioSAXS

The development of functional materials through the formation of supramolecular assemblies is a critical approach in Nature and biomimetics. Here, we will explore the formation of higher-order structures through the directed assembly of α-helical peptides. In particular, the design of the amino acid sequence with non-canonical residues allows the programming of the coiled coils, as shown by our spectroscopic and electron microscopy characterisation. Here, we will perform a detailed determination of the structure of the hierarchical assembly as a function of the peptide architecture, where changes in the size of the side chains control the formation of different oligomers on demand.