Nanoarchitectonics is an emerging field focused on two-dimensional material assemblies and the functionalization of these materials. Self-assembling two-dimensional peptide-based assemblies capable of nanosheet formation, such as collagen mimetic peptides (CMP) and peptoids, have been created, but these peptide-based assemblies have limitations in their controllability. α-helical peptides represent enticing alternatives to CMP and peptoid building blocks due to their higher sequence flexibility and the potential to scale up assembly in vitro. Sheet formations from coiled-coil peptides have not been successful because the helix crossing-angle of 22° prevents tight packing between helices and assembly into two-dimensional structures. On the other hand, research in our lab has shown that straight α-helical peptides are capable of forming two-dimensional nanosheet assemblies stabilized by noncovalent interactions. Through the use of E. coli to express these peptides, the helix length can be extended to allow for the formation of thicker sheets and the peptides can be produced on a larger scale.

Expression and characterization of straight α-helix concatemers for nanosheet formation

251st National Meeting (2016)

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