The potential of supramolecular materials to form programmable assemblies provides a route to fabricate complex materials with desired properties and functionality. One such supramolecular structure is the coiled coil motif, which consists of a peptide strands that form α-helices and self-assemble through hydrophobic effects. The amino acid sequence of the peptides are designed <i>a priori</i> via computational methods and theory to create assembles with desired properties. The resultant coiled-coils are highly robust to both end- and side-group modifications, providing site specific conjugation reactions. End group cysteines and maleimides have been incorporated into a set of antiparallel homotetramer coiled-coil sequences that were subsequently polymerized through a thiol-Michael reaction to form long rigid supramolecular rods. These peptide structures, termed bundlemers, are directly imaged using TEM to reveal rod-like structures having unprecedented aspect ratios of 2 nm width and lengths in excess of 5 µm. Furthermore, external amino acids of the coiled-coil can be selectively substituted with non-natural amino acids for site selective conjugation reactions demonstrating that bundlemers are an excellent substrate for macromolecular design. Specifically, we have incorporated alkyne functionalities along the bundlemers to undergo the copper-catalyze azide-alkyne cycloaddition (CuAAC) click reaction with a variety of structures, such as polymers, nanoparticles, and biological motifs. Such effective tailoring of properties exemplifies bundlemers as a highly effective nanostructural substrate for a variety of applications, including cell-scaffolds, photonics, and drug delivery.

Bundlemers: Supramolecular assembly and functionalization of coiled coils using click chemistry

2019 Spring National Meeting

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