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Alzheimer’s Disease is the most common form of dementia, devastating families around the world. The appearance of neurofibrillary tangles, composed of the protein Tau, are a hallmark of disease progression and correlate to symptom onset. The group is therefore interested in studying approaches to block Tau aggregation and spread to understand mechanisms that may be used for the treatment of Alzheimer’s Disease.


Extracellular monomeric tau protein is sufficient to initiate the spread of tau protein pathology. The group has developed an aggregation sensor based on the fluorescence lifetime of fluorophores attached to Tau; when Tau aggregates the lifetime of the fluorophore drops and can be detected with fluorescence lifetime microscopy (FLIM) (Michel et al., 2014). This method can be used in neuronal models to measure tau aggregation in real-time, and in the presence of pharmacological inhibitors. We use a variety of Tau aggregation paradigms, including the aggregation of monomeric Tau in vitro, upon endocytosis, or expression of Tau in the neuron (AAV, lentivirus). 

We currently study the spread of Tau between cells in microfluidic devices fabricated in the lab, that fluidically isolate neurons connected via their axons. This method can be used to investigate the role of trans-synaptic tau transfer for the progression of tau pathology. We are particularly interested in the mechanisms required for tau propagation in the hope that inhibiting these mechanisms (in collaboration with Dr. Damian Crowther) will help reduce the spread of Tau aggregates through the brain and prevent the progression of AD symptoms.


Neural Cell Models       

E18 Hippocampal Neurons

P1 Dopaminergic Neurons

Differentiated SH-SY5Y cells

Viral Models

Adeno-associated viruses (AAV)


Herpes Simplex Virus (HSV)