Peptide Design and Self-assembly into Targeted Nanostructure and Functional Materials

Peptides have been extensively utilized to construct nanomaterials that display targeted structure through hierarchical assembly. The self-assembly of both rationally designed peptides derived from naturally occurring domains in proteins as well as intuitively or computationally designed peptides that form beta-sheets and helical secondary structures have been widely successful in constructing nanoscale morphologies with well-defined 1-d, 2-d, and 3-d architectures. In this review, we discuss these successes of peptide self-assembly, especially in the context of designing hierarchical materials. In particular, we emphasize the differences in the level of peptide design as an indicator of complexity within the targeted self-assembled materials and highlight future avenues for scientific and technological advances in this field.

Automated summary

Peptides have been extensively used to construct nanomaterials with targeted structures through hierarchical assembly. Both rationally designed peptides derived from natural protein domains and intuitively or computationally designed peptides that form beta-sheets and helical structures have been successful in creating nanoscale morphologies with defined 1-d, 2-d, and 3-d architectures.