Proteins are widely used as nanoscale building blocks to access materials containing inherent enzymatic activity and precise structural properties. However, the heterogeneous surface of proteins introduces difficulties when trying to construct well-defined protein materials due to inherent (non-)specific protein-protein interactions. Most techniques employing protein derivatization introduce synthetic materials or genetic mutations to induce defined protein-protein interactions and construct nanoscale or hierarchical materials. While these are robust approaches to synthesizing protein materials, only recently have proteins been introduced as monomer units assembled into a larger protein polymer chain. Protein polymers introduce the possibility of an expansive functional materials research field when comparing the number of known protein structures to the number of available synthetic monomer units. Furthermore, our group recently demonstrated how the programmability of DNA can be used to precisely polymerize protein monomers via a step-growth or chain-growth process. Importantly, to access morphologies well-known in synthetic polymer assemblies (e.g., lamellae, micelles, vesicles): 1) protein diblock copolymers must be realized; and, 2) the heterogeneous protein surface must be overcome to realize defined assemblies of protein diblock copolymers. This contribution will detail our investigations into the DNA-mediated polymerization of protein diblock copolymers and how we can override the surface heterogeneity of proteins by using metal-coordination chemistry to access bulk and solution protein assemblies only previously realized using synthetic block copolymers.

Programming protein interactions to access protein diblock copolymer assemblies

2019 Fall National Meeting

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