Harnessing the self-assembly of proteins from diverse organisms to build functional materials

Glover D

UNSW Sydney, School of Biotechnology and Biomolecular Sciences.

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 functional materials with nanometer dimensions. This talk will highlight recent engineering and standardisation of modular protein subunits for self-assembly into geometrically defined templates. The central protein building block in the creation of these templates is the gamma-prefoldin (gPFD), a chaperone filament isolated from a hyperthermophilic archaeon. Redesign of the gPFD subunit interface enabled the creation of two and three-way connectors that can link multiple gPFD filaments into macromolecular structures. These protein templates are now being applied to achieve more complex patterning, while expanding the applicability of modular protein templates to diverse enzymatic systems. Fusing different enzymes to each subunit enables periodic positioning of multiple enzymes along the filament to catalyse sequential reactions and metabolic pathways. In addition, metalloproteins can be aligned at high density along filaments to create conductive nanowires. Ultimately, these strategies will enable the design of smart biomaterials for complex applications that require multifunctionalities, such as drug delivery systems, biosensors, and bioelectronic devices.