A New Design of Coiled-Coil Helix Bundle Peptide-Polymer Conjugates

Coiled-coil helix bundles, a common tertiary motif found in many natural proteins, underpins many structural and catalytic functions of natural proteins. \textit{De novo }design has shown that the interior of the helix bundle can be tailored to perform well-defined functions, while the exterior dictates the environment in which it is situated. By attaching synthetic polymers to helix bundle-forming peptides, producing peptide-polymer conjugates, the polymer will mediate the interactions between the helix bundle and its environment, enable the macroscopic self-assembly of the bundles, and potentially, allow them to function in non-biological environments. We report a novel design of peptide-polymer conjugates, where upon attachment of polymer to the exterior of the helix bundle stabilizes the peptide secondary and tertiary structures and preserves the built-in function of the bundle. This new design strategy should be applicable to other coiled-coil peptides and shows great promise as an avenue toward peptide-based biomolecular functional materials.