Dr Margaret Sunde
NHMRC RD Wright Research Fellow G08 - Biochemistry and Microbiology 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.
- Macindoe, I, Glockner, L, Vukasin, P, Stennard, F, Costa, M, Harvey, R, Mackay, J, Sunde, M. Conformational stability and DNA binding specificity of the cardiac T-box transcription factor Tbx20. Journal of molecular biology. 2009; 389:606-18 [Abstract]
- Matthews, J, Bhati, M, Craig, V, Deane, J, Jeffries, C, Lee, C, Nancarrow, A, Ryan, D, Sunde, M. Competition between LIM-binding domains. Biochemical Society Transactions. 2008; 36:1393-1397 [Abstract]
- Kwan, A, Macindoe, I, Vukasin, P, Morris, V, Kass, I, Gupte, R, Mark, A, Templeton, M, Mackay, J, Sunde, M. The Cys3-Cys4 Loop of the Hydrophobin EAS Is Not Required for Rodlet Formation and Surface Activity. Journal of molecular biology. 2008; 382:708-20 [Abstract]
- Sunde, M, Kwan, A, Templeton, M, Beever, R, Mackay, J. Structural analysis of hydrophobins. Micron (Oxford, England : 1993). 2008; 39:773-84 [Abstract]
- 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. 242-243. [Abstract]
- Thorn, D, Ecroyd, H, Sunde, M, Poon, S, Carver, J. Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein. Biochemistry. 2008; 47:3926-36 [Abstract]
- Mackay, J, Sunde, M, Lowry, J, Crossley, M, Matthews, J. Protein interactions: is seeing believing?. Trends in biochemical sciences. 2007. p. 530-1. [Abstract]
- Kirk, E, Sunde, M, Costa, M, Rankin, S, Wolstein, O, Castro, M, Butler, T, Hyun, C, Guo, G, Otway, R, Mackay, J, Waddell, L, Cole, A, Hayward, C, Keogh, A, Macdonald, P, Griffiths, L, Fatkin, D, Sholler, G, Zorn, A, Feneley, M, Winlaw, D, Harvey, R. Mutations in Cardiac T-Box Factor Gene TBX20 Are Associated with Diverse Cardiac Pathologies, Including Defects of Septation and Valvulogenesis and Cardiomyopathy. American journal of human genetics. 2007; 81:280-91 [Abstract]
- Hill, A, Sunde, M, Campbell, T, Vandenberg, J. Mechanism of block of the hERG K+ channel by the scorpion toxin CnErg1. Biophysical journal. 2007; 92:3915-3929 [Abstract]
- Sunde, M, Vandenberg, J, Hill, A. Mechanisms of block of the hERG K+ channel by the scorpion toxin CnErg1. BIOPHYSICAL JOURNAL. 2007; 0:124A-124A [Abstract]
- Ryan, D, Sunde, M, Kwan, A, Marianayagam, N, Nancarrow, A, Vanden Hoven, R, Thompson, L, Baca, M, Mackay, J, Visvader, J, Matthews, J. Identification of the key LMO2-binding determinants on Ldb1. Journal of molecular biology. 2006; 359:66-75 [Abstract]
- Kwan, A, Winefield, R, Sunde, M, Matthews, J, Haverkamp, R, Templeton, M, Mackay, J. Structural basis for rodlet assembly in fungal hydrophobins. Proceedings of the National Academy of Sciences of the United States of America. 2006; 103:3621-6 [Abstract]
- Thorn, D, Meehan, S, Sunde, M, Rekas, A, Gras, S, MacPhee, C, Dobson, C, Wilson, M, Carver, J. Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein. Biochemistry. 2005; 44:17027-36 [Abstract]
- Peto, H, Stott, K, Sunde, M, Broadhurst, R. Backbone dynamics of oxidised and reduced forms of human atrial natriuretic peptide. Journal of structural biology. 2004; 148:214-25 [Abstract]
- Marianayagam, N, Sunde, M, Matthews, J. The power of two: protein dimerization in biology. Trends in biochemical sciences. 2004; 29:618-25 [Abstract]
- Deane, J, Ryan, D, Sunde, M, Maher, M, Guss, J, Visvader, J, Matthews, J. Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex. The EMBO journal. 2004; 23:3589-98 [Abstract]
- Rekas, A, Adda, C, Andrew Aquilina, J, Barnham, K, Sunde, M, Galatis, D, Williamson, N, Masters, C, Anders, R, Robinson, C, Cappai, R, Carver, J. Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity. Journal of molecular biology. 2004; 340:1167-83 [Abstract]
- Sunde, M, McGrath, K, Young, L, Matthews, J, Chua, E, Mackay, J, Death, A. TC-1 is a novel tumorigenic and natively disordered protein associated with thyroid cancer. Cancer research. 2004; 64:2766-73 [Abstract]
- Westman, B, Perdomo, J, Sunde, M, Crossley, M, Mackay, J. The C-terminal domain of Eos forms a high order complex in solution. The Journal of biological chemistry. 2003; 278:42419-26 [Abstract]
- Torres, A, Bansal, P, Sunde, M, Clarke, C, Bursill, J, Smith, D, Bauskin, A, Breit, S, Campbell, T, Alewood, P, Kuchel, P, Vandenberg, J. Structure of the HERG K+ channel S5P extracellular linker: role of an amphipathic alpha-helix in C-type inactivation. The Journal of biological chemistry. 2003; 278:42136-42148 [Abstract]
- Matthews, J, Sunde, M. Zinc fingers--folds for many occasions. IUBMB life. 2002; 54:351-5 [Abstract]
- Jiménez, J, Guijarro, J, Orlova, E, Zurdo, J, Dobson, C, Sunde, M, Saibil, H. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. The EMBO journal. 1999; 18:815-21 [Abstract]
- Sunde, M, Blake, C. From the globular to the fibrous state: protein structure and structural conversion in amyloid formation. Quarterly reviews of biophysics. 1998; 31:1-39 [Abstract]
Neoplasm Proteins; Thyroid Neoplasms