As a structural biologist, I study the structure of proteins at atomic resolution.
By solving the structure of a protein, we learn how the protein functions, its role in disease processes, and how we might modulate it through structure-guided drug design. This makes structural biology an incredibly useful tool in almost all biological fields.
My current research centres on the structure of proteins known to play an important role in neurodegenerative diseases, such as Alzheimer’s disease. One of our most exciting studies is investigating the structure of proteins presented at the surface of microglia, the brain’s immune cells. We are now developing molecules that can target these proteins to improve the ability of microglia to clear the neurotoxic protein aggregates that underpin Alzheimer’s disease.
My work provides opportunities to collaborate with other excellent research teams in Melbourne and beyond. Currently, I collaborate with groups that focus on cancer research, developing new inhibitors that target the proteins controlling gene expression within cancerous cells.
Key achievements
2011 Lorne Conference on Protein Structure and Function, Poster Award
2010 Maurice Wilkins Centre 3-min Thesis Presentation, First Place Award
2009 University of Auckland Doctoral Scholarship
2008 University of Auckland Masters/Honours/PG Dip Scholarship; Biomedical Science Honours Research Symposium Oral Presentation Award
2007 Senior Prize in Biological Sciences
Structural Biology
We determine the three-dimensional atomic structures of proteins involved in disease, with a focus on neurodegenerative diseases and cancer. These structures help us to explore protein function, as well as to discover new drugs.
Lab head: Professor Michael ParkerSelected publications
Baell J.B., Leaver D.J., Hermans S.J., Kelly G.L., Brennan M.S., Downer N.L., Nguyen N., Wichmann J., McRae H.M., Yang Y., Cleary B., Lagiakos H.R., Mieruszynski S., Pacini G., Vanyai H.K., Bergamasco M.I., May R.E., Davey B.K., Morgan K.J., Sealey A.J., Wang B., Zamudio N., Wilcox S., Garnham A.L., Sheikh B.N., Aubrey B.J., Doggett K., Chung M.C., de Silva M., Bentley J., Pilling P., Hattarki M., Dolezal O., Dennis M.L., Falk H., Ren B., Charman S.A., White K.L., Rautela J., Newbold A., Hawkins E.D., Johnstone R.W., Huntington N.D., Peat T.S., Heath J.K., Strasser A., Parker M.W., Smyth G.K., Street I.P., Monahan B.J., Voss A.K., Thomas T., Inhibitors of histone acetyltransferases KAT6A/B induce senescence and arrest tumour growth, Nature, 2018, 560(7717), pp. 253–257. DOI: 10.1038/s41586-018-0387-5
Hermans S.J., Nero T.L., Morton C.J., Gooi J.H., Crespi G.A.N., Hancock N.C., Gao C., Ishii K., Markulić J., Parker M.W., Structural biology of cell surface receptors implicated in Alzheimer’s disease, Biophysical Reviews, 2022, 14(1), pp. 233–255. DOI: 10.1007/s12551-021-00903-9
Crespi G.A., Hermans S.J., Parker M.W., Miles L.A., Molecular basis for mid-region amyloid-β capture by leading Alzheimer’s disease immunotherapies, Scientific Reports, 2015, 5, 9649. DOI: 10.1038/srep09649
Miles L.A., Hermans S.J., Crespi G.A.N., Gooi J.H., Doughty L., Nero T.L., Markulić J., Ebneth A., Wroblowski B., Oehlrich D., Trabanco A.A., Rives M.L., Royaux I., Hancock N.C., Parker M.W., Small Molecule Binding to Alzheimer Risk Factor CD33 Promotes Aβ Phagocytosis, iScience, 2019, 19, pp. 110–118. DOI: 10.1016/j.isci.2019.07.023
Hermans, S.J., Ascher, D.B., Hancock, N.C., Holien J.K., Michell B.J., Chai S.Y., Morton, C.J., Parker, M.W., Crystal structure of human insulin-regulated aminopeptidase with specificity for cyclic peptides, Protein Science, 2015, 24(2), pp. 190–199. DOI: 10.1002/pro.2604
Wong S.W., Vivash L., Mudududdla R., Nguyen N., Hermans S.J., Shackleford D.M., Field J., Xue L., Aprico A., Hancock N.C., Haskali M., Stashko M.A., Frye S.V., Wang X., Binder M.D., Ackermann U., Parker M.W., Kilpatrick T.J., Baell J.B., Development of [18F]MIPS15692, a radiotracer with in vitro proof-of-concept for the imaging of MER tyrosine kinase (MERTK) in neuroinflammatory disease, European Journal of Medicinal Chemistry, 2021, 226, 113822. DOI: 10.1016/j.ejmech.2021.113822
ORCID profile: https://orcid.org/0000-0002-2513-5054