Dominic J. Glover*

 

School of Biotechnology and Biomolecular Sciences, The University of New South Wales, Sydney, Australia.

 

The fabrication of nanoscale devices requires architectural templates on which to position functional molecules in complex arrangements. Protein scaffolds are particularly promising templates for nanomaterials due to inherent molecular recognition and self-assembly capabilities combined with genetically encoded functionalities1. This talk will highlight recent engineering of a filamentous protein for self-assembly into geometrically defined templates of tunable dimensions and symmetry2. The central protein building block in the creation of these templates is the g-prefoldin (gPFD), a chaperone filament isolated from a hyperthermophilic archaeon3,4. Redesign of the gPFD subunit interface enabled the creation of two and three-way connectors that can link multiple gPFD filaments into complex structures2. These protein templates are now being applied to achieve more complex patterning, while expanding the applicability of gPFD 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, cytochrome C proteins can be aligned at high density along filaments as a first step to creating novel 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.

1.Glover, D. J. & Clark, D. S. ACS Central Sciences 2016, 2, 438–444. Protein calligraphy: A new concept begins to take shape.

2.Glover, D. J. et al. Nature Communications 2016, 7, 11771. Geometrical assembly of ultrastable protein templates for nanomaterials.

3. Glover, D. J. et al. Biotechnology Journal 2013, 8, 228-236. Engineering protein filaments with enhanced thermostability for nanomaterials.

4.Glover, D. J. & Clark, D. S. FEBS Journal 2015, 282, 2985-2997. Oligomeric assembly is required for chaperone activity of the filamentous γ-prefoldin.

 

Biographic Details

Name: Dominic J. Glover

Title: Dr

Affiliation, Country: Senior Lecturer, School of Biotechnology and Biomolecular Sciences, The University of New South Wales, Sydney, Australia.

Phone: +61 2 9385 3382, Email: d.glover@unsw.edu.au

Research interests: Protein design and engineering, Synthetic biology, biomaterials, Self-assembly, Biocatalysis, Extremophiles

Venue

Room: 
AEB 301