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Transcript
Proteins as supramolecular building blocks: towards active nanoscaffolds Juliet A. Gerrard 1, Tong Zhu 1, Grant Pearce 1 2 1 Mac Diarmid Institute and Biomolecular Interaction Centre, University of Canterbury The last decade has witnessed a huge gain in understanding of the way in which small molecules can be assembled into discrete and polymeric 1, 2 and 3D architectures. Key challenges remain before this knowledge can be harnessed in nanoscale devices. Integral to these challenges is the question of scale: well characterised self-assembling systems typically use components of 1 -2 nm dimensions, whilst nanoscale devices demand 10-100 nm. In this research, we aim to bridge the scale gap by using proteins as our building blocks. We are u sing the methods of protein engineering to assemble non-native quaternary st ructures and active nanoscaffolds. Two model systems are being explored: a TIM barrel enzyme, representing the most common protein fold and therefore scaffold for activity; and the peroxiredoxins, a family of proteins that have already revealed themselves to have unique self-assembly properties controlled by a redox switch. Non-native architectures have been obtained and progress is being made in the controlled assembly of these structures using ligand triggered assembly or changes in redox properties of the solvent. Specifically: the assembly of the TIM-barrel protein may be controlled by the binding of pyruvate; and the assembly of an expressed peroxiredoxin can be controlled by a single mutation at the interface. This is a promising approach for the assembly of active materials on the nanoscale, as we refine the triggered assembly and disassembly of these st ructures by an environmental trigger and expand the repertoire of chemical and biological activities incorporated into the scaffold.