Dr Margaret Sunde
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NHMRC RD Wright Research Fellow Biochemistry Faculty of Science G08 - Biochemistry Building
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The formation of stable, fibrillar protein assemblies is associated with many disease states, including Alzheimer's disease and Type II diabetes. These are non-functional deposits. Protein aggregates that have similar structural features but which are functional have been identified in several microorganisms. In these cases the self-assembly of the protein is advantageous to the organism. For example, hydrophobins are fungal proteins that self-assemble in an ordered manner into amphipathic films at air:water interfaces. They reduce the surface tension at air:water boundaries and form very hydrophobic coatings on fungal spore surfaces which facilitate dispersal in air. Hydrophobin assemblies share the ordered b sheet structural core that has been characterized in amyloid deposits. We are interested in studying the biophysical and structural basis for the self-assembly of hydrophobins and other amyloidogenic proteins.
Hydrophobin monolayer formation is a unique system that combines protein self-assembly with the generation of functional surfaces. These remarkable properties suggest a range of commercial applications, including biocompatibility enhancement of medical implants and emulsion and dispersion applications in foods and pharmaceuticals. This project involves using mutagenesis to probe the effect of sequence on hydrophobin structure and the study of the self-assembly process with techniques such as fluorescence, nuclear magnetic resonance, X-ray fibre diffraction and electron microscopy. Our work aims to develop a detailed picture of hydrophobin organisation within surface films. We hope to manipulate the self-assembly properties of the hydrophobins for the rational design of novel biological polymers and to design molecules that inhibit fungal spore dispersal and colonisation.
Hydrophobin monolayer formation is a unique system that combines protein self-assembly with the generation of functional surfaces. These remarkable properties suggest a range of commercial applications, including biocompatibility enhancement of medical implants and emulsion and dispersion applications in foods and pharmaceuticals. This project involves using mutagenesis to probe the effect of sequence on hydrophobin structure and the study of the self-assembly process with techniques such as fluorescence, nuclear magnetic resonance, X-ray fibre diffraction and electron microscopy. Our work aims to develop a detailed picture of hydrophobin organisation within surface films. We hope to manipulate the self-assembly properties of the hydrophobins for the rational design of novel biological polymers and to design molecules that inhibit fungal spore dispersal and colonisation.
Current national competitive grants
| 2008 | |
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A novel approach to fighting fungal infections: targeted disruption of hydrophobin monolayers Sunde M, Kwan A, Tovey E. |
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| Australian Research Council (ARC) Discovery Project | $244,251 over 3 years |
2008
Mackay, J, Sunde, M, Lowry, J, Crossley, M, Matthews, J. Response to Chatr-aryamontri et al.: Protein interactions: to believe or not to believe?. Trends in biochemical sciences. 2008. p. 242-3. [Abstract]
2007
Mackay, J, Sunde, M, Lowry, J, Crossley, M, Matthews, J. Protein interactions: is seeing believing?. Trends in biochemical sciences. 2007. p. 530-531. [Abstract]
Sunde, M, Kwan, A, Templeton, M, Beever, R, Mackay, J. Structural analysis of hydrophobins. Micron (Oxford, England : 1993). 2007: 1-12 [Abstract]
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