Associate Professor Margaret Sunde

Associate Professor
Pharmacology, School of Medical Sciences

Telephone +61 2 9351 6955
Fax +61 2 9351 3868

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Research interests

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 beta-sheet structural core that has been characterized in amyloid deposits.

Hydrophobin assemblies shield the human pathogenic fungus Aspergillus fumigatus from the immune response during infection, allowing this fungus to go on to cause life-threatening invasive aspergillosis. In rice blast, the most important fungal disease of rice, infection of the plants is facilitated by the production of a hydrophobin layer by the fungus Magnaporthe grisea. We are therefore interested in studying the biophysical and structural basis for the self-assembly of hydrophobins, with a view to understanding the role played by these proteins in fungal infections. 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.

PhD and master's project opportunities

Selected grants

2014

  • Regional flow cytometry facility; Sunde M, Olsson M; Australian Research Council (ARC)/Linkage Infrastructure, Equipment and Facilities (LIEF).
  • CLARIOstar Multifunctional Microplate Reader for Shared Used at the Open Access, Multi-User Molecular Biology Core Facility; Huang M, Scolyer R, Fraser S, Sahni S, Speranza T, Owens T, Barrs V, Ju Y, Kovacevic Z, Lu Z, Camp A, Slobedman B, Morris B, Oliver B, Dos Remedios C, Kalinowski D, Fu D, Lai D, Lovicu F, Allbutt H, Triccas J, Burgess J, Kril J, Dixon K, Rendina L, Byrne M, King N, Groundwater P, Williamson P, Ho J, Dong Q, Bao B, Assinder S, McLennan S, Richardson D, Ammit A, Sharland A, Hardikar A, Hong A, Hambly B, Lee C, Murphy C, Goldsbury C, Johnstone D, Lane D, Hibbs D, Joshua D, Huq F, Halliday G, Sutherland G, Zreiqat H, Lok H, Lyons G, Jansson P, Black J, Zhu L, Sunde M, Day M, Naylor M, Buckland M, Murray M, Shafie N, Lay P, Poronnik P, Codd R, Mason R, Ryan R, Christopherson R, de Graaf S; National Health and Medical Research Council (NHMRC)/Equipment Grants.

2013

  • Preparation of selectively labelled and deuterated hydrophobin proteins for solid-state NMR; Kwan A, Sunde M; Australian Institute of Nuclear Science and Engineering (AINSE)/Awards.
  • The Nanotemper: State-of-the-art instrumentation for the characterization of protein interactions; Payne R, Matthews J, Ataide S, Campbell I, Weiss A, Sunde M, Mackay J; Clive and Vera Ramaciotti Foundations/Awards for Biomedical Research: Major Equipment.
  • Multiangle laser light scattering instrument for protein characterisation; Mackay J, Ataide S, Jormakka M, Ryan R, Matthews J, Shepherd N, Sunde M, Collyer C, Payne R; National Health and Medical Research Council (NHMRC)/Equipment Grants.
  • Robotic High Throughput Western Analysis for the Open Access, Multi-User Sydney Cancer Research Core Facility; Richardson D, Scolyer R, Boyer M, Halliday G, Damian D, Christopherson R, Joshua D, Kench J, Hong A, Murray M, Lee C, Kalinowski D, Naylor M, Lay P, Lyons G, Kovacevic Z, Mason R, Dixon K, Chan-Ling T, Hawkins C, Sunde M, Lovejoy D, Owens T, Rendina L, Jansson P, Dos Remedios C, Charles (nee Slaviero) K, Lane D, Witting P, Dong Q, Ammit A, Groundwater P, Assinder S, Bao B, Byrne S, Zhou F, Buckland M, Grewal T, Huq F, Lai D, Codd R, Zhang D, Fu D, de Graaf S, Huang M, Payne R, Slobedman B, Barrs V, Ho J, Williamson P, Murphy C; DVC Research/Equipment Grant.

2012

  • Breaching the defences: the role of hydrophobin protein monolayers in rice blast fungal infections; Sunde M, Kwan A; Australian Research Council (ARC)/Discovery Projects (DP).
  • Integrated Facility for Confocal Imaging and Single Molecule Fluorescence Analysis; Yerbury J, Olsson M, Sunde M, Campbell I, Truscott R; Australian Research Council (ARC)/Linkage Infrastructure, Equipment and Facilities (LIEF).

2011

  • POLARStar Omega; Sunde M, Guss M, Mackay J, Matthews J, Payne R, Cubeddu L; National Health and Medical Research Council (NHMRC)/Equipment Grants.
  • Shared resource for protein discovery; Matthews J, Mabbutt B, Brown L, Paulsen I, Stock D, Sunde M, Trewhella J; Australian Research Council (ARC)/Linkage Infrastructure, Equipment and Facilities (LIEF).

2010

  • Functional and biophysical analysis of hydrophobins from Aspergillus fumigatus; Sunde M, Latge J; Department of Innovation, Industry, Science and Research (Federal)/International Science Linkages (ISL) Competitive Grants.
  • Exploiting the self-assembly of hydrophobin proteins to engineer functional nanostructuring surfaces; Sunde M, Kwan A, Yang W; Australian Research Council (ARC)/Discovery Projects (DP).
  • A Unique Soft Matter High-Performance Scanning Probe Microscopy (HP-SPM) Facility; Thordarson P, Neto C, Warr G, Coster H, Weiss A, Perrier S, Hawkett B, Bilek M, Sunde M, Harris A; Australian Research Council (ARC)/Linkage Infrastructure, Equipment and Facilities (LIEF).
  • Automated Microwave accelerated Solid Phase Peptide Synthesizer; Jolliffe K, Payne R, Hambley T, Mackay J, Sunde M; National Health and Medical Research Council (NHMRC)/Equipment Grants.

2009

  • Applied Biosystems 7500 Fast Real Time PCR system; Campbell I, Crossley P, Brand-Miller J, Caterson I, Hall R, Weiss A, Conigrave A, Mackay J, Matthews J, Sunde M, Gell D, Bell-Anderson K, Nicholas H, Crossett B; National Health and Medical Research Council (NHMRC)/Equipment Grants.

2008

  • A novel approach to fighting fungal infections: targeted disruption of hydrophobin monolayers; Sunde M, Kwan A, Tovey E; Australian Research Council (ARC)/Discovery Projects (DP).

2007

  • Manipulating the self assembly properties of fungal hydrophobin proteins for the design of novel bio; Sunde M, Kwan A, Mackay J; Australian Research Council (ARC)/Linkage Projects (LP).
  • Characterization and inhibition of self-assembly by fungal hydrophobin proteins; Sunde M; University of Sydney/Career Interruption.

2006

  • Structural Basis For The Regulation Of Cardiac Gene Transcription By T-Box Transcription Factors; Sunde M; National Health and Medical Research Council (NHMRC)/Established Career Fellowships.

Selected publications

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Book Chapters

  • Morris, V., Sunde, M. (2013). Formation of Amphipathic Amyloid Monolayers from Fungal Hydrophobin Proteins. In Juliet A. Gerrard (Eds.), Protein Nanotechnology: Protocols, Instrumentation, and Applications, (pp. 119-129). New York: Humana Press.
  • Matthews, J., Sunde, M. (2012). Dimers, Oligomers, Everywhere. In Jacqueline M Matthews (Eds.), Protein Dimerization and Oligomerization in Biology, (pp. 1-18). New York: Springer Science + Business Media.
  • Sunde, M., Templeton, M., Kwan, A. (2012). Fungal Fibrils: Application of the Amyloid Polymer Structure by Fungi. In Suzi Jarvis and Anika Mostaert (Eds.), The Functional Fold: Amyloid Structures in Nature, (pp. 35-54). Singapore: Pan Stanford Publishing.

Journals

  • Ren, Q., Kwan, A., Sunde, M. (2014). Solution structure and interface-driven self-assembly of NC2, a new member of the class II hydrophobin proteins. Proteins: Structure, Function, and Bioinformatics, 82(6), 990-1003. [More Information]
  • Morris, V., Kwan, A., Sunde, M. (2013). Analysis of the Structure and Conformational States of DewA Gives Insight into the Assembly of the Fungal Hydrophobins. Journal of Molecular Biology, 425(2), 244-256. [More Information]
  • Rey, A., Hocher, A., Kwan, A., Sunde, M. (2013). Backbone and sidechain 1H, 13C and 15N chemical shift assignments of the hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae. Biomolecular NMR Assignments, 7(1), 109-112. [More Information]
  • Yang, W., Ren, Q., Wu, Y., Morris, V., Rey, A., Braet, F., Kwan, A., Sunde, M. (2013). Surface Functionalization of Carbon Nanomaterials by Self-Assembling Hydrophobin Proteins. Biopolymers : Peptide Science, 99(1), 84-94. [More Information]
  • Ren, Q., Kwan, A., Sunde, M. (2013). Two forms and two faces, multiple states and multiple uses: Properties and applications of the self-assembling fungal hydrophobins. Biopolymers : Peptide Science, 100(6), 601-612. [More Information]
  • Morris, V., Kwan, A., Mackay, J., Sunde, M. (2012). Backbone and sidechain 1H, 13C and 15N chemical shift assignments of the hydrophobin DewA from Aspergillus nidulans. Biomolecular N M R Assignments, 8, 83-86. [More Information]
  • Bayry, J., Aimanianda, V., Inaki Guijarro, J., Sunde, M., Latge, J. (2012). Hydrophobins-Unique Fungal Proteins. PLoS Pathogens, 8(5), 1-4. [More Information]
  • Simone, A., Kitchen, C., Kwan, A., Sunde, M., Dobson, C., Frenkel, D. (2012). Intrinsic disorder modulates protein self-assembly and aggregation. Proceedings of the National Academy of Sciences (PNAS) of the United States of America, 109(18), 6951-6956. [More Information]
  • Healy, J., Wong, K., Sawyer, E., Roux, C., Domigan, L., Gras, S., Sunde, M., Larsen, N., Gerrard, J., Vasudevamurthy, M. (2012). Polymorphism and higher order structures of protein nanofibers from crude mixtures of fish lens crystallins: Toward useful materials. Biopolymers : Peptide Science, 97(8), 595-606. [More Information]
  • Macindoe, I., Kwan, A., Ren, Q., Morris, V., Yang, W., Mackay, J., Sunde, M. (2012). Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS. Proceedings of the National Academy of Sciences (PNAS) of the United States of America, 109(14), E804-E811. [More Information]
  • Finn, T., Nunez, A., Sunde, M., Easterbrook-Smith, S. (2012). Serum albumin prevents protein aggregation and amyloid formation and retains chaperone-like activity in the presence of physiological ligands. Journal of Biological Chemistry, 287(25), 21530-21540. [More Information]
  • Morris, V., Linser, R., Wilde, K., Duff, A., Sunde, M., Kwan, A. (2012). Solid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural Heterogeneity. Angewandte Chemie (International Edition), 51(50), 12621-12625. [More Information]
  • Morris, V., Ren, Q., Macindoe, I., Kwan, A., Byrne, N., Sunde, M. (2011). Recruitment of Class I Hydrophobins to the Air: Water Interface Initiates a Multi-step Process of Functional Amyloid Formation. Journal of Biological Chemistry, 286(18), 15955-15963. [More Information]
  • Posch, M., Gramlich, M., Sunde, M., Schmitt, K., Lee, S., Richter, S., Kersten, A., Perrot, A., Panek, A., Al Khatib, I., et al (2010). A Gain-of-function TBX20 Mutation Causes Congenital Atrial Septal Defects, Patent Foramen Ovale and Cardiac Valve Defects. Journal of Medical Genetics, 47(4), 230-235. [More Information]
  • Macindoe, I., Glockner, L., Vukasin, P., Stennard, F., Costa, M., Harvey, R., Mackay, J., Sunde, M. (2009). Conformational stability and DNA binding specificity of the cardiac T-box transcription factor Tbx20. Journal of Molecular Biology, 389(3), 606-618. [More Information]
  • Adda, C., Murphy, V., Sunde, M., Waddington, L., Schloegel, J., Talbo, G., Vingas, K., Kienzle, V., Masciantonio, R., Howlett, G., et al (2009). Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrils. Molecular and Biochemical Parasitology, 166(2), 159-171. [More Information]
  • Thorn, D., Ecroyd, H., Sunde, M., Poon, S., Carver, J. (2008). Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein. Biochemistry, 47(12), 3926-3936. [More Information]
  • Matthews, J., Bhati, M., Craig, V., Deane, J., Jeffries, C., Lee, C., Nancarrow, A., Ryan, D., Sunde, M. (2008). Competition between LIM-binding domains. Biochemical Society Transactions, 36(6), 1393-1397. [More Information]
  • Kwan, A., Macindoe, I., Vukasin, P., Morris, V., Kass, I., Gupte, R., Mark, A., Templeton, M., Mackay, J., Sunde, M. (2008). The Cys3-Cys4 Loop of the Hydrophobin EAS Is Not Required for Rodlet Formation and Surface Activity. Journal of Molecular Biology, 382, 708-720. [More Information]
  • Hill, A., Sunde, M., Campbell, T., Vandenberg, J. (2007). Mechanism of block of the hERG K+ channel by the scorpion toxin CnErg1. Biophysical Journal, 92(11), 3915-3929. [More Information]
  • Kirk, E., Sunde, M., Costa, M., Rankin, S., Wolstein, O., Castro, M., Butler, T., Hyun, C., Guo, G., Otway, R., Mackay, J., Sholler, G., Winlaw, D., et al (2007). 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, 81(2), 280-291. [More Information]
  • Mackay, J., Sunde, M., Lowry, J., Crossley, P., Matthews, J. (2007). Protein interactions: is seeing believing? Trends in Biochemical Sciences, 32(12), 530-531. [More Information]
  • Sunde, M., Kwan, A., Templeton, M., Beever, R., Mackay, J. (2007). Structural analysis of hydrophobins. Micron, doi:10.1016/j.micron.2007.08.003, 1-12. [More Information]
  • Ryan, D., Sunde, M., Kwan, A., Marianayagam, N., Nancarrow, A., vanden Hoven, R., Thompson, L., Baca, M., Mackay, J., Visvader, J., Matthews, J. (2006). Identification of the key LMO2-binding determinants on Ldb1. Journal of Molecular Biology. [More Information]
  • Kwan, A., Winefield, R., Sunde, M., Matthews, J., Haverkamp, R., Templeton, M., Mackay, J. (2006). Structural basis for rodlet assembly in fungal hydrophobins. Proceedings of the National Academy of Sciences (PNAS) of the United States of America, 103(10), 3621-3626. [More Information]
  • Thorn, D., Meehan, S., Sunde, M., Rekas, A., Gras, S., MacPhee, C., Dobson, C., Wilson, M., Carver, J. (2005). Amyloid Fibril Formation by Bovine Milk kappa-Casein and Its Inhibition by the Molecular Chaperones alpha(s)- and beta-Casein. Biochemistry, 44(51), 17027-17036. [More Information]
  • Peto, H., Stott, K., Sunde, M., Broadhurst, R. (2004). Backbone dynamics of oxidised and reduced forms of human atrial natriuretic peptide. Journal of Structural Biology, 148(2), 214-225.
  • Sunde, M. (2004). Book Review: Protein misfolding and disease: Principles and protocols. Methods in molecular biology,. Protein Science, 13(6), 1704-1705.
  • Rekas, A., Adda, C., Aquilina, J., Barnham, K., Sunde, M., Galatis, D., Williamson, N., Masters, C., Anders, R., Robinson, C., Carver, J., et al (2004). Interaction Of The Molecular Chaperone Alpha B-Crystallin With Alpha-Synuclein: Effects On Amyloid Fibril Formation And Chaperone Activity. Journal of Molecular Biology, 340(5), 1167-1183. [More Information]
  • Deane, J., Ryan, D., Sunde, M., Maher, M., Guss, M., Visvader, J., Matthews, J. (2004). Tandem Lim Domains Provide Synergistic Binding In The LMO4:Ldb1 Complex. The EMBO Journal, 23(18), 3589-3598.
  • Sunde, M., McGrath, K., Young, L., Matthews, J., Chua, E., Mackay, J., Heather, A. (2004). Tc-1 Is A Novel Tumorigenic And Natively Disordered Protein Associated With Thyroid Cancer. Cancer Research, 64(8), 2766-2773.
  • Marianayagam, N., Sunde, M., Matthews, J. (2004). The Power Of Two: Protein Dimerization In Biology. Trends in Biochemical Sciences, 29(11), 618-625.
  • Smith, D., Jones, S., Serpell, L., Sunde, M., Radford, S. (2003). A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation. Journal of Molecular Biology, 330(5), 943-954.
  • Andreola, A., Bellotti, V., Giorgetti, S., Mangione, P., Obici, L., Stoppini, M., Torres, J., Monzani, E., Merlini, G., Sunde, M. (2003). Conformational switching and fibrillogenesis in the amyloidogenic fragment of apolipoprotein a-I. Journal of Biological Chemistry, 278(4), 2444-2451.
  • Torres, A., Bansal, P., Sunde, M., Clarke, C., Bursill, J., Smith, D., Bauskin, A., Breit, S., Campbell, T., Alewood, P., Kuchel, P., et al (2003). Structure of the HERG K+ channel S5P extracellular linker. Role of an amphipathic alpha-Helix in C-type inactivation. Journal of Biological Chemistry, 278(43), 42136-42148.
  • Westman, B., Perdomo, J., Sunde, M., Crossley, P., Mackay, J. (2003). The C-terminal domain fo Eos forms a high order complex in solution. Journal of Biological Chemistry, 278(43), 42419-42426.
  • Canet, D., Last, A., Tito, P., Sunde, M., Spencer, A., Archer, D., Redfield, C., Robinson, C., Dobson, C. (2002). Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nature Structural and Molecular Biology, 9(4), 308-315.
  • Matthews, J., Sunde, M. (2002). Zinc fingers- folds for many occasions. IUBMB Life, 54(6), 351-355.
  • Mangione, P., Sunde, M., Giorgetti, S., Stoppini, M., Esposito, G., Gianelli, L., Obici, L., Asti, L., Andreola, A., Viglino, P., et al (2001). Amyloid fibrils derived from the apolipoprotein A1 Leu174Ser variant contain elements of ordered helical structure. Protein Science, 10(1), 187-199.

Conferences

  • Marianayagam, N., Sunde, M., Matthews, J. (2004). Biophysical Characterization Of The Interaction Of Ldb1 With Lm02.

2014

  • Ren, Q., Kwan, A., Sunde, M. (2014). Solution structure and interface-driven self-assembly of NC2, a new member of the class II hydrophobin proteins. Proteins: Structure, Function, and Bioinformatics, 82(6), 990-1003. [More Information]

2013

  • Morris, V., Kwan, A., Sunde, M. (2013). Analysis of the Structure and Conformational States of DewA Gives Insight into the Assembly of the Fungal Hydrophobins. Journal of Molecular Biology, 425(2), 244-256. [More Information]
  • Rey, A., Hocher, A., Kwan, A., Sunde, M. (2013). Backbone and sidechain 1H, 13C and 15N chemical shift assignments of the hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae. Biomolecular NMR Assignments, 7(1), 109-112. [More Information]
  • Morris, V., Sunde, M. (2013). Formation of Amphipathic Amyloid Monolayers from Fungal Hydrophobin Proteins. In Juliet A. Gerrard (Eds.), Protein Nanotechnology: Protocols, Instrumentation, and Applications, (pp. 119-129). New York: Humana Press.
  • Yang, W., Ren, Q., Wu, Y., Morris, V., Rey, A., Braet, F., Kwan, A., Sunde, M. (2013). Surface Functionalization of Carbon Nanomaterials by Self-Assembling Hydrophobin Proteins. Biopolymers : Peptide Science, 99(1), 84-94. [More Information]
  • Ren, Q., Kwan, A., Sunde, M. (2013). Two forms and two faces, multiple states and multiple uses: Properties and applications of the self-assembling fungal hydrophobins. Biopolymers : Peptide Science, 100(6), 601-612. [More Information]

2012

  • Morris, V., Kwan, A., Mackay, J., Sunde, M. (2012). Backbone and sidechain 1H, 13C and 15N chemical shift assignments of the hydrophobin DewA from Aspergillus nidulans. Biomolecular N M R Assignments, 8, 83-86. [More Information]
  • Matthews, J., Sunde, M. (2012). Dimers, Oligomers, Everywhere. In Jacqueline M Matthews (Eds.), Protein Dimerization and Oligomerization in Biology, (pp. 1-18). New York: Springer Science + Business Media.
  • Sunde, M., Templeton, M., Kwan, A. (2012). Fungal Fibrils: Application of the Amyloid Polymer Structure by Fungi. In Suzi Jarvis and Anika Mostaert (Eds.), The Functional Fold: Amyloid Structures in Nature, (pp. 35-54). Singapore: Pan Stanford Publishing.
  • Bayry, J., Aimanianda, V., Inaki Guijarro, J., Sunde, M., Latge, J. (2012). Hydrophobins-Unique Fungal Proteins. PLoS Pathogens, 8(5), 1-4. [More Information]
  • Simone, A., Kitchen, C., Kwan, A., Sunde, M., Dobson, C., Frenkel, D. (2012). Intrinsic disorder modulates protein self-assembly and aggregation. Proceedings of the National Academy of Sciences (PNAS) of the United States of America, 109(18), 6951-6956. [More Information]
  • Healy, J., Wong, K., Sawyer, E., Roux, C., Domigan, L., Gras, S., Sunde, M., Larsen, N., Gerrard, J., Vasudevamurthy, M. (2012). Polymorphism and higher order structures of protein nanofibers from crude mixtures of fish lens crystallins: Toward useful materials. Biopolymers : Peptide Science, 97(8), 595-606. [More Information]
  • Macindoe, I., Kwan, A., Ren, Q., Morris, V., Yang, W., Mackay, J., Sunde, M. (2012). Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS. Proceedings of the National Academy of Sciences (PNAS) of the United States of America, 109(14), E804-E811. [More Information]
  • Finn, T., Nunez, A., Sunde, M., Easterbrook-Smith, S. (2012). Serum albumin prevents protein aggregation and amyloid formation and retains chaperone-like activity in the presence of physiological ligands. Journal of Biological Chemistry, 287(25), 21530-21540. [More Information]
  • Morris, V., Linser, R., Wilde, K., Duff, A., Sunde, M., Kwan, A. (2012). Solid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural Heterogeneity. Angewandte Chemie (International Edition), 51(50), 12621-12625. [More Information]

2011

  • Morris, V., Ren, Q., Macindoe, I., Kwan, A., Byrne, N., Sunde, M. (2011). Recruitment of Class I Hydrophobins to the Air: Water Interface Initiates a Multi-step Process of Functional Amyloid Formation. Journal of Biological Chemistry, 286(18), 15955-15963. [More Information]

2010

  • Posch, M., Gramlich, M., Sunde, M., Schmitt, K., Lee, S., Richter, S., Kersten, A., Perrot, A., Panek, A., Al Khatib, I., et al (2010). A Gain-of-function TBX20 Mutation Causes Congenital Atrial Septal Defects, Patent Foramen Ovale and Cardiac Valve Defects. Journal of Medical Genetics, 47(4), 230-235. [More Information]

2009

  • Macindoe, I., Glockner, L., Vukasin, P., Stennard, F., Costa, M., Harvey, R., Mackay, J., Sunde, M. (2009). Conformational stability and DNA binding specificity of the cardiac T-box transcription factor Tbx20. Journal of Molecular Biology, 389(3), 606-618. [More Information]
  • Adda, C., Murphy, V., Sunde, M., Waddington, L., Schloegel, J., Talbo, G., Vingas, K., Kienzle, V., Masciantonio, R., Howlett, G., et al (2009). Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrils. Molecular and Biochemical Parasitology, 166(2), 159-171. [More Information]

2008

  • Thorn, D., Ecroyd, H., Sunde, M., Poon, S., Carver, J. (2008). Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein. Biochemistry, 47(12), 3926-3936. [More Information]
  • Matthews, J., Bhati, M., Craig, V., Deane, J., Jeffries, C., Lee, C., Nancarrow, A., Ryan, D., Sunde, M. (2008). Competition between LIM-binding domains. Biochemical Society Transactions, 36(6), 1393-1397. [More Information]
  • Kwan, A., Macindoe, I., Vukasin, P., Morris, V., Kass, I., Gupte, R., Mark, A., Templeton, M., Mackay, J., Sunde, M. (2008). The Cys3-Cys4 Loop of the Hydrophobin EAS Is Not Required for Rodlet Formation and Surface Activity. Journal of Molecular Biology, 382, 708-720. [More Information]

2007

  • Hill, A., Sunde, M., Campbell, T., Vandenberg, J. (2007). Mechanism of block of the hERG K+ channel by the scorpion toxin CnErg1. Biophysical Journal, 92(11), 3915-3929. [More Information]
  • Kirk, E., Sunde, M., Costa, M., Rankin, S., Wolstein, O., Castro, M., Butler, T., Hyun, C., Guo, G., Otway, R., Mackay, J., Sholler, G., Winlaw, D., et al (2007). 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, 81(2), 280-291. [More Information]
  • Mackay, J., Sunde, M., Lowry, J., Crossley, P., Matthews, J. (2007). Protein interactions: is seeing believing? Trends in Biochemical Sciences, 32(12), 530-531. [More Information]
  • Sunde, M., Kwan, A., Templeton, M., Beever, R., Mackay, J. (2007). Structural analysis of hydrophobins. Micron, doi:10.1016/j.micron.2007.08.003, 1-12. [More Information]

2006

  • Ryan, D., Sunde, M., Kwan, A., Marianayagam, N., Nancarrow, A., vanden Hoven, R., Thompson, L., Baca, M., Mackay, J., Visvader, J., Matthews, J. (2006). Identification of the key LMO2-binding determinants on Ldb1. Journal of Molecular Biology. [More Information]
  • Kwan, A., Winefield, R., Sunde, M., Matthews, J., Haverkamp, R., Templeton, M., Mackay, J. (2006). Structural basis for rodlet assembly in fungal hydrophobins. Proceedings of the National Academy of Sciences (PNAS) of the United States of America, 103(10), 3621-3626. [More Information]

2005

  • Thorn, D., Meehan, S., Sunde, M., Rekas, A., Gras, S., MacPhee, C., Dobson, C., Wilson, M., Carver, J. (2005). Amyloid Fibril Formation by Bovine Milk kappa-Casein and Its Inhibition by the Molecular Chaperones alpha(s)- and beta-Casein. Biochemistry, 44(51), 17027-17036. [More Information]

2004

  • Peto, H., Stott, K., Sunde, M., Broadhurst, R. (2004). Backbone dynamics of oxidised and reduced forms of human atrial natriuretic peptide. Journal of Structural Biology, 148(2), 214-225.
  • Marianayagam, N., Sunde, M., Matthews, J. (2004). Biophysical Characterization Of The Interaction Of Ldb1 With Lm02.
  • Sunde, M. (2004). Book Review: Protein misfolding and disease: Principles and protocols. Methods in molecular biology,. Protein Science, 13(6), 1704-1705.
  • Rekas, A., Adda, C., Aquilina, J., Barnham, K., Sunde, M., Galatis, D., Williamson, N., Masters, C., Anders, R., Robinson, C., Carver, J., et al (2004). Interaction Of The Molecular Chaperone Alpha B-Crystallin With Alpha-Synuclein: Effects On Amyloid Fibril Formation And Chaperone Activity. Journal of Molecular Biology, 340(5), 1167-1183. [More Information]
  • Deane, J., Ryan, D., Sunde, M., Maher, M., Guss, M., Visvader, J., Matthews, J. (2004). Tandem Lim Domains Provide Synergistic Binding In The LMO4:Ldb1 Complex. The EMBO Journal, 23(18), 3589-3598.
  • Sunde, M., McGrath, K., Young, L., Matthews, J., Chua, E., Mackay, J., Heather, A. (2004). Tc-1 Is A Novel Tumorigenic And Natively Disordered Protein Associated With Thyroid Cancer. Cancer Research, 64(8), 2766-2773.
  • Marianayagam, N., Sunde, M., Matthews, J. (2004). The Power Of Two: Protein Dimerization In Biology. Trends in Biochemical Sciences, 29(11), 618-625.

2003

  • Smith, D., Jones, S., Serpell, L., Sunde, M., Radford, S. (2003). A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation. Journal of Molecular Biology, 330(5), 943-954.
  • Andreola, A., Bellotti, V., Giorgetti, S., Mangione, P., Obici, L., Stoppini, M., Torres, J., Monzani, E., Merlini, G., Sunde, M. (2003). Conformational switching and fibrillogenesis in the amyloidogenic fragment of apolipoprotein a-I. Journal of Biological Chemistry, 278(4), 2444-2451.
  • Torres, A., Bansal, P., Sunde, M., Clarke, C., Bursill, J., Smith, D., Bauskin, A., Breit, S., Campbell, T., Alewood, P., Kuchel, P., et al (2003). Structure of the HERG K+ channel S5P extracellular linker. Role of an amphipathic alpha-Helix in C-type inactivation. Journal of Biological Chemistry, 278(43), 42136-42148.
  • Westman, B., Perdomo, J., Sunde, M., Crossley, P., Mackay, J. (2003). The C-terminal domain fo Eos forms a high order complex in solution. Journal of Biological Chemistry, 278(43), 42419-42426.

2002

  • Canet, D., Last, A., Tito, P., Sunde, M., Spencer, A., Archer, D., Redfield, C., Robinson, C., Dobson, C. (2002). Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nature Structural and Molecular Biology, 9(4), 308-315.
  • Matthews, J., Sunde, M. (2002). Zinc fingers- folds for many occasions. IUBMB Life, 54(6), 351-355.

2001

  • Mangione, P., Sunde, M., Giorgetti, S., Stoppini, M., Esposito, G., Gianelli, L., Obici, L., Asti, L., Andreola, A., Viglino, P., et al (2001). Amyloid fibrils derived from the apolipoprotein A1 Leu174Ser variant contain elements of ordered helical structure. Protein Science, 10(1), 187-199.

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