The intricate and ordered complexes that proteins adopt in nature is central to many biological processes, ranging from cellular scaffolding provided by cytoskeletal proteins to the encapsulation of nucleic acids in viral capsids. Exploiting this remarkable fidelity and precision in self-assembly is highly attractive for the fabrication of structurally defined materials with nanometer dimensions. Advances in the computational prediction of protein folding have enabled the design of proteins that self-assemble into complex yet predictable shapes.
My research applies synthetic biology for the engineering of proteins into structured and functional biomaterials. Central to this approach is the creation of standardised protein building blocks composed of ultrastable filamentous proteins and connectors that assemble into geometrically-defined structures of controllable size and shape. This ability to design protein nanostructures with atomic-level accuracy opens new possibilities in biomaterials. Initial applications of this technology include the creation of electrically conductive protein nanowires for biosensors and enzyme catalysis, the engineering of metabolic pathways, and the fabrication of tissue scaffolds for regenerative medicine.
Current collaborations include Professor Doug Clark (UC Berkeley), A/Professor Allon Hochbaum (UC Irvine), A/Professor Nicholas Stephanopoulos (Biodesign Institute, Arizona State University), and A/Professor Lisa Martin (Monash University).