<br/>Some of the most complex peptide assembly in nature is carried out using the lipid bilayer as a foundation for controlling local chemical environment. The bilayer provides well-defined nonpolar regions, as well as controlling the locations of specific functional groups in the membrane periphery. The noncovalent interactions between amphiphiles in the bilayer also enables amphiphiles to be displaced, enabling expansion of growing peptide structures in the membrane. While amphiphiles form standing phases in the cell membrane, they can also be assembled to form striped phases on materials such as graphene and highly oriented pyrolytic graphite (HOPG). In the striped phase, the alkyl chains extend horizontally across the substrate, creating a surface that looks like a repeating cross-section of a lipid bilayer, with 1-nm-wide stripes of functional headgroups alternating with 5-nm-wide stripes of hydrophobic alkyl chains. We will discuss experiments and simulations illustrating that striped phases represent a means of controlling assembly of peptides and amino acids at interfaces, both utilizing the stripes of functional headgroups, and using the amphiphiles as a displaceable template that balances alkyl-alkyl and alkyl-pi interactions on the aromatic substrate.<br/>

Peptide assembly at interfaces templated by striped phases of amphiphiles

2019 Fall National Meeting

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