(590f) A Modular, Biomimetic Strategy for the Synthesis of Nanoscale Inorganic Materials

In natural systems, a single protein can be used to perform multiple functions by interacting with other proteins at well-defined epitope binding sites to form a variety of functional co-assembled structures. Inspired by the biological use of epitope recognition to enable diverse yet specific functions, we developed Template Engineering Through Epitope Recognition (TEThER), a strategy that takes advantage of noncovalent, molecular recognition between different components to achieve functional versatility from a single protein template. Engineered TEThER peptides are rationally designed to serve as molecular bridges between protein epitope binding sites and inorganic materials in a localized, specific, and versatile manner. These bifunctional peptides include protein recognition sequences that noncovalently bind to specific sites on the protein scaffold and inorganic recognition sequences that serve as sites for localized bio-enabled nucleation and growth of inorganic materials.

Here we functionalized self-assembled clathrin protein cages at specific sites through co-assembly with designed TEThER peptides to achieve nanostructures with three tailored chemical functionalities: the bio-enabled synthesis of gold, cobalt oxide, and anatase titanium dioxide nanoparticles in aqueous solvents at room temperature and ambient pressure. Compared with previous demonstrations of bio-enabled inorganic synthesis, the TEThER strategy relies solely on defined, noncovalent interactions without requiring any genetic or chemical modifications to the protein template. Therefore, this design strategy represents a mix-and-match, biomimetic approach to achieve versatile and site-specific functionalization that can be broadly applied to other protein templates to generate structures with a range of functionalities.