Vanessa Morris

Senior LecturerVanessa Morris

Julius von Haast 422
Internal Phone: 90532


Research Interests

My lab is focused on studying the structures, mechanisms and interactions of aggregating proteins. We are particularly interested in a certain fibre-like structure that is formed by a great variety of proteins called amyloid fibrils. We study amyloid proteins involved in disease, including Alzheimer's disease and motor neuron disease, as well as those that have functions in important biological processes.

The kinds of questions we are looking at include:
1) What are the functions of amyloids and aggregates in different biological processes?
2) What are the structural details of aggregates that have functional and disease-relevant roles?
3) How do other proteins and small molecules affect the aggregation of disease-relevant proteins, and at what stage do they affect aggregation? 4) What sequences are important for aggregation processes, and how can these be interfered with?
5) How do disease mutations affect aggregation or functional behaviour of aggregation-prone proteins?

We studying these topics with a range of structural and biophysical techniques including NMR spectroscopy (both solid-state and solution state), fluorescence-based aggregation assays, electron microscopy.

For more info, check out our webpage at

Recent Publications

  • Harper AR., Dobson RCJ., Morris VK. and Moggré GJ. (2022) Fermentation of plant-based dairy alternatives by lactic acid bacteria. Microbial Biotechnology 15(5): 1404-1421.
  • Smyth LCD., Murray HC., Hill M., van Leeuwen E., Highet B., Magon NJ., Osanlouy M., Mathiesen SN., Mockett B. and Singh-Bains MK. (2022) Neutrophil-vascular interactions drive myeloperoxidase accumulation in the brain in Alzheimer’s disease. Acta Neuropathologica Communications 10(1)
  • Göbl C., Morris VK., van Dam L., Visscher M., Polderman PE., Hartlmüller C., de Ruiter H., Hora M., Liesinger L. and Birner-Gruenberger R. (2020) Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A. Redox Biology 28
  • Brender JR., Ghosh A., Kotler SA., Krishnamoorthy J., Bera S., Morris V., Sil TB., Garai K., Reif B. and Bhunia A. (2019) Probing transient non-native states in amyloid beta fiber elongation by NMR. Chemical Communications 55(31): 4483-4486.
  • Sun Y., Medina Cruz A., Hadley KC., Galant NJ., Law R., Vernon RM., Morris VK., Robertson J. and Chakrabartty A. (2019) Physiologically Important Electrolytes as Regulators of TDP-43 Aggregation and Droplet-Phase Behavior. Biochemistry 58(6): 590-607.