Professor Margaret Sunde
Academic Director Sydney Analytical Core Research Facility
Margie Sunde is currently a Professor in the School of Medical Sciences at the University of Sydney. She completed her undergraduate studies in Biochemistry at the University of Cape Town, then moved in 1990 to undertake a PhD in the lab of Hal Dixon in Biochemistry at the University of Cambridge. In 1993 she started a postdoc with Colin Blake at the Laboratory of Molecular Biophysics in Oxford, where she developed her interest in amyloid fibrils associated with disease. Using X-ray fibre diffraction and crystallography, she studied both the amyloid fibril structure and the soluble forms of amyloidogenic protein precursors. This work contributed to the growing understanding that all amyloid fibrils share a common underlying beta sheet structure and that amyloid formation associated with disease involves protein misfolding. Following that, she held a Medical Research Council Research Fellowship with Prof Sir Chris Dobson FRS, looking specifically at protein misfolding in amyloid diseases and then started her own group back in Cambridge in 1998, as a Royal Society University Research Fellow. Margie moved to Australia and took a career-break in 2001, with periods of part-time work until 2005. In 2006 she started her research program focused on the structure and formation of functional amyloid structures in microorganisms, in particular amyloids with a biological role in infection or immune evasion.
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.
We have recently discovered that certain viral proteins can inhibit the host programmed cell death pathway necroptosis. This occurs by formation of heteromeric amyloids fibrils composed of both viral and host proteins that contain the amyloidogenic sequences known as RHIMs (RIP Homotypic Interaction Motifs). The Sunde group has applied single molecule methods to characterise these hetero-amyloids and to reveal this novel viral sequestration of host proteins and the molecular basis for viral inhibition of RHIM-based signalling in mammalian cells. This project aims to investigate the structural basis for different types of RHIM amyloid assembly associated with necroptosis in response to insult and under pathological conditions, such as neurodegeneration, ischemia and microbial infection.
Margie Sunde's teaching interests include drugs for treatment of conditions associated with cardiovascular disease, including antihypertensives, lipid-lowering therapies, novel delivery methods for diabetes drugs and the development of effective protein therapeutics.
1. Understanding the structural basis and impact of functional amyloid assembly within the programmed cell death pathway necroptosis.
2. Targeting functional amyloid assemblies that contribute to fungal infectivity and pathogenesis.
3. Super-resolution imaging of pathological and functional amyloid structures.
Member of the Australian Research Council College of Experts (2020-2022)
2019: Awarded the Australian Biophysics Society Bob Robertson Medal for Outstanding Career Achievements in Biophysics.http://www.biophysics.org.au/br_award.html
Afghanistan | (Columbia University) Collaboration with Professor Ann McDermott: ssNMR studies of functional amyloid fibrils involved in host defense against viral infection. |
France | (Pasteur Institut, Paris) Collaborative research into the role of functional amyloids in the human pathogenic fungus Aspergillus fumigatus. |
Spain | (Rocasolano Institute of the Spanish National Research Council) Dr Miguel Mompean: Investigation of the dynamic assembly of functional amyloids involved in programmed cell death. |
United Kingdom | (The University of Edinburgh) Partnership Collaboration Award 2019: Fluorescent sensors for super-resolution microscopy to revolutionise the imaging of neurodegeneration. |
| Project title | Research student |
|---|---|
| Harnessing the inflammatory power of necroptosis to build second-generation viral oncolytic vectors | Olivia LAVIDIS |
| Design of biomaterials from peptide self-assembly | Tianchen LI |
| Protein condensates for mRNA recruitment and delivery | Benedict TAI |
Publications
Book Chapters
- Ball, S., Pham, C., Lo, V., Morris, V., Kwan, A., Sunde, M. (2020). Formation of Amphipathic Amyloid Monolayers from Fungal Hydrophobin Proteins. In Juliet A. Gerrard, Laura J Domigan (Eds.), Protein Nanotechnology: Protocols, Instrumentation, and Applications: Third Edition, (pp. 55-72). New York: Springer. [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. [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. [More Information]
Journals
- Heath, S., Gray, S., Hamzah, E., O’Connor, K., Bozonet, S., Botha, A., de Cordovez, P., Magon, N., Naughton, J., Goldsmith, D., Sunde, M., et al (2024). Amyloid formation and depolymerization of tumor suppressor p16INK4a are regulated by a thiol-dependent redox mechanism. Nature Communications, 15(1). [More Information]
- Sullivan, M., Lane, S., McKenzie, A., Ball, S., Sunde, M., Neely, G., Moreno, C., Maximova, A., Werry, E., Kassiou, M. (2024). iPSC-derived PSEN2 (N141I) astrocytes and microglia exhibit a primed inflammatory phenotype. Journal of Neuroinflammation, 21(1). [More Information]
- Kumar, M., Teakel, S., Swarbrick, C., Chowdhury, I., Thorn, D., Sunde, M., Carver, J., Forwood, J. (2023). Amyloid fibril formation, structure and domain swapping of acyl-coenzyme A thioesterase-7. FEBS Journal, 290(16), 4057-4073. [More Information]
Conferences
- Marianayagam, N., Sunde, M., Matthews, J. (2004). Biophysical Characterization Of The Interaction Of Ldb1 With Lm02.
2024
- Heath, S., Gray, S., Hamzah, E., O’Connor, K., Bozonet, S., Botha, A., de Cordovez, P., Magon, N., Naughton, J., Goldsmith, D., Sunde, M., et al (2024). Amyloid formation and depolymerization of tumor suppressor p16INK4a are regulated by a thiol-dependent redox mechanism. Nature Communications, 15(1). [More Information]
- Sullivan, M., Lane, S., McKenzie, A., Ball, S., Sunde, M., Neely, G., Moreno, C., Maximova, A., Werry, E., Kassiou, M. (2024). iPSC-derived PSEN2 (N141I) astrocytes and microglia exhibit a primed inflammatory phenotype. Journal of Neuroinflammation, 21(1). [More Information]
2023
- Kumar, M., Teakel, S., Swarbrick, C., Chowdhury, I., Thorn, D., Sunde, M., Carver, J., Forwood, J. (2023). Amyloid fibril formation, structure and domain swapping of acyl-coenzyme A thioesterase-7. FEBS Journal, 290(16), 4057-4073. [More Information]
- Pham, C., Titaux-Delgado, G., Varghese, N., Polonio, P., Wilde, K., Sunde, M., Mompeán, M. (2023). NMR characterization of an assembling RHIM (RIP homotypic interaction motif) amyloid reveals a cryptic region for self-recognition. Journal of Biological Chemistry, 299(4). [More Information]
- Ball, S., Adamson, J., Sullivan, M., Zimmermann, M., Lo, V., Sanz-Hernandez, M., Jiang, X., Kwan, A., McKenzie, A., Werry, E., Kassiou, M., Rutledge, P., Sunde, M., et al (2023). Perphenazine-Macrocycle Conjugates Rapidly Sequester the Aβ42 Monomer and Prevent Formation of Toxic Oligomers and Amyloid. ACS Chemical Neuroscience, 14(1), 87-98. [More Information]
2022
- Kaur, A., Adair, L., Ball, S., New, E., Sunde, M. (2022). A Fluorescent Sensor for Quantitative Super-Resolution Imaging of Amyloid Fibril Assembly. Angewandte Chemie - International Edition, 61(10), e202112832-1-e202112832-6. [More Information]
- Bahraminejad, E., Paliwal, D., Sunde, M., Holt, C., Carver, J., Thorn, D. (2022). Amyloid fibril formation by α
S1 - and β-casein implies that fibril formation is a general property of casein proteins. Biochimica et Biophysica Acta. Proteins and Proteomics, 1870 (11-12). [More Information] - Bursill, C., Smith, N., Palpant, N., Tan, I., Sunde, M., Harvey, R., Lewis, B., Figtree, G., Vandenberg, J. (2022). Don't Turn Off the Tap! The Importance of Discovery Science to the Australian Cardiovascular Sector and Improving Clinical Outcomes Into the Future. Heart, Lung, and Circulation, 31(10), 1321-1332. [More Information]
2021
- Shanmugam, N., Baker, M., Sanz-Hernandez, M., Sierecki, E., Gambin, Y., Steain, M., Pham, C., Sunde, M. (2021). Herpes simplex virus encoded ICP6 protein forms functional amyloid assemblies with necroptosis-associated host proteins. Biophysical Chemistry, 269, 106524. [More Information]
- Thorn, D., Bahraminejad, E., Grosas, A., Koudelka, T., Hoffmann, P., Mata, J., Devlin, G., Sunde, M., Ecroyd, H., Holt, C., et al (2021). Native disulphide-linked dimers facilitate amyloid fibril formation by bovine milk αₛ₂-casein. Biophysical Chemistry, 270, 106530. [More Information]
- Graziotto, M., Adair, L., Kaur, A., Vérité, P., Ball, S., Sunde, M., Jacquemin, D., New, E. (2021). Versatile naphthalimide tetrazines for fluorogenic bioorthogonal labelling. RSC Chemical Biology, 2(5), 1491-1498. [More Information]
2020
- Siddiquee, R., Choi, S., Lam, S., Wang, P., Qi, R., Otting, G., Sunde, M., Kwan, A. (2020). Cell-free expression of natively folded hydrophobins. Protein Expression and Purification, 170, 1-7. [More Information]
- Ball, S., Pham, C., Lo, V., Morris, V., Kwan, A., Sunde, M. (2020). Formation of Amphipathic Amyloid Monolayers from Fungal Hydrophobin Proteins. In Juliet A. Gerrard, Laura J Domigan (Eds.), Protein Nanotechnology: Protocols, Instrumentation, and Applications: Third Edition, (pp. 55-72). New York: Springer. [More Information]
- Ball, S., Kwan, A., Sunde, M. (2020). Hydrophobin Rodlets on the Fungal Cell Wall. Current Topics in Microbiology and Immunology, 425, 29-51. [More Information]
2019
- Valsecchi, I., Lai, J., Stephen-Victor, E., Pille, A., Beaussart, A., Lo, V., Pham, C., Aimanianda, V., Kwan, A., Duchateau, M., Sunde, M., et al (2019). Assembly and disassembly ofergillus fumigatus conidial rodlets. The Cell Surface, 5, 1-21. [More Information]
- Lo, V., Lai, J., Sunde, M. (2019). Fungal Hydrophobins and Their Self-Assembly into Functional Nanomaterials. Advances in Experimental Medicine and Biology, 1174, 161-185. [More Information]
- Shanmugam, N., Baker, M., Ball, S., Steain, M., Pham, C., Sunde, M. (2019). Microbial functional amyloids serve diverse purposes for structure, adhesion and defence. Biophysical Reviews, 11(3), 287-302. [More Information]
2018
- Pham, C., Rodriguez de Francisco, B., Valsecchi, I., Dazzoni, R., Pille, A., Lo, V., Ball, S., Cappai, R., Wien, F., Kwan, A., Sunde, M., et al (2018). Probing Structural Changes during Self-assembly of Surface-Active Hydrophobin Proteins that Form Functional Amyloids in Fungi. Journal of Molecular Biology, 430(20), 3784-3801. [More Information]
2017
- Lo, V., Kwan, A., Sunde, M. (2017). Altering Hydrophobin Film with Ethanol: Controlling the Self Assembly of Hydrophobin Films. Imaging & Microscopy, 4, 1-4.
- Pearson, J., Giogha, C., Muhlen, S., Nachbur, U., Pham, C., Zhang, Y., Hildebrand, J., Oates, C., Lung, T., Ingle, D., Sunde, M., et al (2017). EspL is a bacterial cysteine protease effector that cleaves RHIM proteins to block necroptosis and inflammation. Nature Microbiology, 2, 1-9. [More Information]
- Sunde, M., Pham, C., Kwan, A. (2017). Molecular Characteristics and Biological Functions of Surface-Active and Surfactant Proteins. Annual Review of Biochemistry, 86, 585-608. [More Information]
2016
- Kulminskaya, N., Vasa, S., Giller, K., Becker, S., Kwan, A., Sunde, M., Linser, R. (2016). Access to side-chain carbon information in deuterated solids under fast MAS through non-rotor-synchronized mixing. Chemical Communications, 52(2), 268-271. [More Information]
- Constantine, M., Liew, C., Lo, V., Macmillan, A., Cranfield, C., Sunde, M., Whan, R., Graham, R., Martinac, B. (2016). Heterologously-expressed and Liposome-reconstituted Human Transient Receptor Potential Melastatin 4 Channel (TRPM4) is a Functional Tetramer. Scientific Reports, 6, 1-11. [More Information]
- Pham, C., Rey, A., Lo, V., Soules, M., Ren, Q., Meisl, G., Knowles, T., Kwan, A., Sunde, M. (2016). Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism. Scientific Reports, 6, 1-16. [More Information]
2015
- Pille, A., Kwan, A., Sunde, M., Cheung, I., Hampsey, M., Aimanianda, V., Delepierre, M., Latge, J., Inaki Guijarro, J. (2015). (1)H, (13)C and (15)N resonance assignments of the RodA hydrophobin from the opportunistic pathogen Aspergillus fumigatus. Biomolecular NMR Assignments, 9(1), 113-118. [More Information]
2014
- Pham, C., Kwan, A., Sunde, M. (2014). Functional amyloid: widespread in Nature, diverse in purpose. Essays in Biochemistry, 56(1), 207-219. [More Information]
- Lo, V., Ren, Q., Pham, C., Morris, V., Kwan, A., Sunde, M. (2014). Fungal Hydrophobin Proteins Produce Self-Assembling Protein Films with Diverse Structure and Chemical Stability. Nanomaterials, 4(3), 827-843. [More Information]
- Linser, R., Bardiaux, B., Andreas, L., Hyberts, S., Morris, V., Pintacuda, G., Sunde, M., Kwan, A., Wagner, G. (2014). Solid-State NMR Structure Determination from Diagonal-Compensated, Sparsely Nonuniform-Sampled 4D Proton-Proton Restraints. Journal of the American Chemical Society, 136(31), 11002-11010. [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. [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. [More Information]
- 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. [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]
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 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. [More Information]
- 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.
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. [More Information]
- 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. [More Information]
- 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. [More Information]
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. [More Information]
- Matthews, J., Sunde, M. (2002). Zinc fingers- folds for many occasions. IUBMB Life, 54(6), 351-355. [More Information]
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.
Selected Grants
2023
- Rewarding Research 2024, Sunde M, Faculty of Medicine and Health/FMH Rewarding Research Success
- Eliminating implant biofilms, Kwan A, Yeo G, Gao J, Sunde M, Nano Institute/Kickstarter
2022
- Collaborative project on chronic traumatic encephalopathy (CTE), Sunde M, Sydney Local Health District/Research Support
- Australian Peptide Display Facility, Payne R, Passioura T, Mackay J, Sunde M, Gale P, Australian Research Council (ARC)/Linkage Infrastructure, Equipment and Facilities (LIEF)