Peptides comprised entirely of beta-amino acids, or beta-peptides, have attracted substantial interest over the past 25 years due to their unique structural and chemical characteristics. beta-Peptides form well-defined secondary structures that exhibit different geometries compared with their alpha-peptide counterparts, giving rise to their foldamer classification. beta-Peptide foldamers can be functionalized easily and are metabolically stable and, together with the predictable side-chain topography, have led to the design of a growing number of bioactive beta-peptides with a range of biological targets. The strategic engineering of chemical and topographic properties has also led to the design of beta-peptide mimics of higher-order oligomers. More recently, the ability of these peptides to self-assemble into complex structures of controlled geometries has been exploited in materials applications. The focus of this mini-review is on how the unique structural features of beta-peptide assemblies have been exploited in the design of self-assembled proteomimetic bundles and nanomaterials.
Gopalan, R. D., Del Borgo, M. P., Mechler, A. I., Perlmutter, P., & Aguilar, M-I. I. (2015). Geometrically precise building blocks: the self-assembly of beta-peptides. Chemistry and Biology, 22(11), 1417 - 1423. https://doi.org/10.1016/j.chembiol.2015.10.005