Inspired by the structural precision and functionality of transmembrane proteins, we have pursued a strategy for organizing α-helix bundles into liquid crystalline periodic arrays. Organization of the peptide nanostructures into periodic arrays within these peptide-polymer films provides access to detailed information about the structure of the peptide in this abiological environment. While strategies to organize linear dipeptides and peptide macrocycles are well established, little attention has been paid to organizing helical proteins or α-helix bundles into liquid crystalline mesophases. Conjugating polymers to these peptides can augment the properties of peptides to afford solution-processable materials for use as free-standing films or conformal coatings. We have pursued the idea that the α-helix bundle structure will be stabilized in columnar mesophases by shape complementarity with flat-tapered dendrons. Combining sequence-defined peptides with amphiphilic dendrons affords tremendous control over the primary, secondary, and quaternary structure of self-organized α-helix bundles. The presentation will discuss the interplay between folding, assembly, and self-organization of α-helix bundles in thermotropic liquid crystalline mesophases and opportunities to utilize this platform for rationally controlling hierarchical organization in bulk, nanostructured materials.

Bio-inspired arrays of dendronized α-helix bundle assemblies

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.