Rate My Professor Sarah Heath

Sarah Heath is a PhD candidate in the Department of Pathology and Biomedical Science, University of Otago Christchurch, Faculty of Medicine, Health Sciences Division. She holds a Bachelor of Biomedical Sciences with Honours (BBiomedSc(Hons)) from the University of Otago, completing her honours thesis in 2018 on 'Intracellular redox changes during TNFα-mediated necroptosis' under supervisor Mark Hampton. Her current PhD research at the Mātai Hāora - Centre for Redox Biology and Medicine (previously Centre for Free Radical Research) focuses on the molecular mechanisms of p16INK4a amyloid formation. Supervised by Dr Christoph Göbl, Dr Vanessa K. Morris, and collaborators, Heath has demonstrated that oxidation of cysteines in the tumor suppressor p16INK4a promotes rapid formation of amyloid fibrils through a partially structured disulfide-bonded dimeric intermediate. This process is fully reversible upon disulfide reduction, revealing a thiol-dependent redox mechanism that governs amyloid assembly and disassembly. This positions p16INK4a as a functional redox switch, potentially active during the S-phase of the cell cycle, with significant relevance given p16INK4a's frequent mutations in various cancers.

Heath is first author on the seminal 2024 Nature Communications paper 'Amyloid formation and depolymerization of tumor suppressor p16INK4a are regulated by a thiol-dependent redox mechanism,' showing cancer-associated mutations increase amyloid propensity while stabilizing mutations inhibit it. Additional peer-reviewed publications include co-authorship on 'Characterizing the amyloid core region of the tumor suppressor protein p16INK4a using a limited proteolysis and peptide-based approach' (Journal of Biological Chemistry, 2024), 'Oxidation of caspase-8 by hypothiocyanous acid enables TNF-mediated necroptosis' (2023), 'Molecular basis of a redox switch: molecular dynamics simulations and surface plasmon resonance provide insight into reduced and oxidised angiotensinogen' (2021), and 'Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2' (2021). She has presented her work verbally and via posters at the 32nd Society for Redox Research Australasia Meeting, 34th Queenstown Molecular Biology Meeting, and Queenstown Research Week Biomolecular Interactions Meeting. Funded by the Royal Society Marsden Fund and Health Research Council of New Zealand, her contributions advance understanding of redox biology in cancer, with potential impacts on diagnostics and treatments, as highlighted in University of Otago news.