Polymers, which are structurally related to polypeptides, are a subject of scientific interest, because they are generally considered suitable for biomedical and biotechnological applications.
Poly(peptoid)s are N-substituted poly(amide)s and therefore don’t exhibit hydrogen bonding interactions along the backbone. Moreover, they do not contain a peptide-like sidechain at the Cα and therefore lack stereogenic centers. Both mentioned structural differences compared to the isomeric peptides affect the self-assembly behavior drastically and enable the design of exceptional secondary structures and self-assemblies.
In the past, attention has been drawn mostly towards the poly(α-peptoids), which are N-substituted poly(glycine)s. The β- and γ-analogs, which contain an additional methylene or ethylene unit in the backbone, respectively, comparatively little is known, presumably because synthesis protocols are challenging. Optimization of synthesis protocols would permit the development of a new library containing amphiphilic block copoly(peptoid)s and would allow investigation of structure-property relationships.
Specifically, the synthesis of di- and triblock copoly(peptoid)s will be addressed and the self-assembly behavior of the synthesized polymers discussed.