Encapsulation and compartmentalization are key features of living systems. An ability to mimic this via designed peptides would provide a unique route towards new materials for delivery, and the development of encapsulated complex systems. Recently, we have made use of the coiled coil; a fold in which two or more α-helices self-associate about a central hydrophobic core. As one of the most well-understood protein folds, we utilized a number of design rules 1 to produce a pair of robustly-folded assemblies: a parallel homotrimer; and a heterodimer. Tethering these together in a back-to-back fashion produces two 6-stranded hubs which, when combined, produce a network of tessellated hexagons. Moreover, owing to the symmetry of this system, any inherent curvature (as indicated by molecular dynamics simulations) would result in enclosed objects. Indeed, when the homotrimer—heterodimer peptides were mixed a fine precipitate was observed, which, following Scanning Electron Microscopy was shown to be composed of uniform spherical objects 97 ± 19 nm (n=135) in diameter. Further analysis by Atomic Force Microscopy confirmed the spherical nature of these objects in the hydrated state, which were seen to collapse to ~9 nm in height when dehydrated providing evidence for hollow structures. Startlingly, images obtained using Lateral Molecular Force Microscopy revealed details of a hexagonal surface structure consistent with the design. More recently, we have explored factors contributing to the formation of the cages: by making single point mutations to our coiled-coil building blocks we can affect both curvature and the stage at which closure occurs, furnishing populations of larger and smaller nanocages, respectively. This work has recently been published 2 and reviewed 3 .