ANM
2010
3rd
International Conference on Advanced Nano Materials
12-15 September 2010 - Agadir, Morocco
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Abstract
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ANMM117 |
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AMYLOID FIBRILS AS CONDUCTING NANOWIRES |
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L. J. Domigan (1,2), S. J. Meade (3), R. J. Blaikie (2,4) and J. A. Gerrard (1,2) |
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(1) School of Biological Sciences, University of Canterbury, New Zealand
(2) MacDiarmid Institute for Advanced Materials and Nanotechnology, New Zealand
(3) powerHouse, Canterbury, New Zealand
(4) Department of Electrical and Computer Engineering, University of Canterbury, New Zealand. |
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Amyloid
fibril is the name given to the insoluble fibrous quaternary structure
formed by the assembly of normally soluble protein or peptide monomers
into intermolecularly hydrogen bonded β-sheets. Best known for
their role in a number of diseases, research into amyloid fibrils now
includes their potential as nanomaterials and components, due to them
possessing a number of favourable properties such as self-assembly,
strength and stability.
This research is investigating amyloid fibrils as conducting nanowires.
Conductivity of amyloid fibrils from native protein sources was
measured via by dispersal over microfabricated interdigitated electrode
arrays, and it was seen that while the native fibrils have low
conductivity, this can be increased by up to five orders of magnitude
through the formation of amyloid-conducting polymer conjugates. Control
over the dimensions of these protein nanowires further increases their
desirability as nanomaterials, and results from research aimed at
achieving this will also be presented.
Another aim is to recognise new opportunities for amyloid fibrils in
the fields of biosensing, through immobilisation of glucose oxidase to
the amyloid fibril scaffold, with preliminary research showing a
significant change in current in the presence of glucose. Future
research intends to further explore the biosensing potential of amyloid
fibrils, along with potential applications in other areas of
nanoelectronics. |
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