We demonstrate here that rationally designed block copolypeptides based on poly(L‐arginine) and β‐sheet peptides can form toroidal nanostructures. In aqueous solution, we found that 1D nanoribbons roll up and connect in an end‐to‐end fashion under charge‐balanced conditions, resulting in the formation of barrel‐like toroidal nanostructures. Toroidal diameter was highly uniform (10 nm), indicating that there is a preferred geometrical packing requirement for toroid formation. Our results demonstrate that, when suitably designed, β‐sheet nanostructures can be manipulated to form more complex 2D nanostructures. This finding offers new opportunities not only for the fabrication of more sophisticated peptide‐based nanobiomaterials, but also for understanding and inhibiting protein misfolding diseases.