UC San Diego

Whether for constructing advanced materials and complex biological devices, or for building sophisticated coordination complexes with diverse metal-based functions, proteins are Nature's favorite building blocks. Yet, our ability to control the assembly of proteins or to use them as ligand platforms for inorganic chemistry has been somewhat limited. The goal of this thesis was to exploit the utility of a protein scaffold in both regards. First, by considering proteins as "simple" ligand platforms and controlling the metal coordination chemistry on their surfaces, we show how their self-assembly can be readily dictated by metal binding. Next, we show how having this measure of control can lead to the site-specifically localization of functional metal complexes on the surface of a proteins and peptides. While on one hand our studies have pointed out the challenges of using proteins as ligands, they have also revealed how extensive and chemically-rich protein surfaces can be