Current success in foldamer design has stemmed from several biosimilar foldamer backbones that borrow several design choices from traditional biopolymers. Using peptide or phospodiester linkers allows researchers to start with a working design that has been evolutionarily selected to fold under certain conditions. These biopolymers include interactions such as hydrogen bonds in protein backbones, or π-stacking and base-pair hydrogen bonds in nucleic acids. Biosimilar foldamers also take advantage of preexisting synthesis techniques allowing comparatively quick synthesis compared to a novel backbone synthesis. Despite their similarity to existing biopolymers, these biosimilar foldamers are still considerably difficult to design. In order to facilitate the foldamer design process, new ways to propose potentially stable foldamers chemistries are needed. Better tools to formulate novel foldamers would help discover new backbone chemistries that are not biologically inspired. New computational tools to validate new foldamer chemistries would also help incentivise the use of more difficult synthetic techniques.