top of page

Mudher Lab

Copy of Copy of Visualising dementia poster draft (1).png
Drosophila Or47b by Amber Cooper

Research

The research interests of the lab revolve around dissecting the mechanisms by which neuronal dysfunction and degeneration occurs in neurodegenerative diseases, especially in tauopathies such as Alzheimer’s disease.

​

The over-arching aim is to use this knowledge both for identification of disease-modifying drug targets and for generation of novel, “patient-specific” diagnostic tools that may enable earlier diagnosis and improved disease stratification.

​

To achieve this, a number of experimental paradigms are employed to model aspects of tauopathy in vitro and in vivo, and a range of biochemical and biophysical methodologies are utilized to study the ensuing pathological processes.

​

Interdisciplinary research is a central theme running through many projects in the lab, mediated through collaborations with other Drosophila biologists (Prof. Doug Allan, UBC Canada and Prof. Makis Skoulakis, Alexander Fleming Institute, Greece), biophysicists (Prof. Sumeet Mahajan, UoS), structural biologists (Prof. Phil Williamson, UoS) and clinicians (Prof. Chris Kipps, UoS).

News & Events

Mudher interview BBC SolentArtist Name
00:00 / 06:59

Latest Publications

Aggidis, A. et al. (2024) ‘A novel peptide-based tau aggregation inhibitor as a potential therapeutic for Alzheimer’s disease and other tauopathies’, Alzheimer’s & dementia: the journal of the Alzheimer’s Association. Wiley, 20(11), pp. 7788–7804. doi: 10.1002/alz.14246.

As aggregation underpins Tau toxicity, aggregation inhibitor peptides may have disease-modifying potential. They are therefore currently being designed and target either the 306VQIVYK311 aggregation-promoting hotspot found in all Tau isoforms or the 275VQIINK280 aggregation-promoting hotspot found in 4R isoforms. However, for any Tau aggregation inhibitor to potentially be clinically relevant for other tauopathies, it should target both hotspots to suppress aggregation of Tau isoforms, be stable, cross the blood-brain barrier, and rescue aggregation-dependent Tau phenotypes in vivo.

CyberCanyon.jpg
bottom of page