Composed of only twenty amino acids, proteins offer complex functions and impressive binding capabilities. Synthetic polymers offer an expansive monomer scope yielding tunable chemical and physical properties. Building on the strengths of both classes of macromolecules, we have designed several hybrid architectures.

We have leveraged small synthetic oligomers to control the assembly of peptides using peptide-polymer amphiphiles. The morphology and dynamics of the assembled nanomaterial can be tuned using properties of the synthetic tail. Complementarily, we have leveraged peptides as a pendent group on synthetic polymers to generate local rigidity analogous to secondary structure in synthetic random copolymers. As secondary structure is critical for protein function, this local rigidity impacts the function the synthetic polymer.

These efforts are motivated by both developing a deeper understanding of the impact of secondary structure on protein properties and developing functional scalable materials that can target global challenges in sustainability such as industrial separations and water purification.