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Department of Chemical Engineering and Biotechnology

 

Currently researching the role of the protein alpha-synuclein (aSyn) in Parkinson's Disease. As a monomer aSyn is an intrinsically disordered protein with no tertiary structure, but during disease an unknown trigger can initiate aSyn's misfolding where it forms into oligomers and subsequently highly structured beta-sheet containing fibrils, a hallmark of Parkinson's Disease. It's physiological role is still unclear, but is thought to be involved in the recycling and homeostasis of synaptic vesicles in neurons.  

Specific research topics involve, (i) understanding the physiological role of aSyn and it's interaction with synaptic vesicles. (ii) how aSyn becomes pathogenic during aggregation and what happens to the synaptic vesicles during this process. (iii) how the surrounding environmental can influence the misfolding propensity of monomeric aSyn leading it to aggregate, particularly focussing on the role of ions and water mobility. 

C-terminal calcium binding of a-synuclein modulated synaptic vesicle interactions. Nat Comms. (2018) https://www.nature.com/articles/s41467-018-03111-4

The cellular environment affects monomeric a-synuclein structure. TIBS. (2019) https://www.sciencedirect.com/science/article/pii/S0968000418302469

Research

Dr. Amberley Stephens is a Post Doc in the Molecular Neuroscience Group, having completed a PhD in molecular microbiology. Her role includes cloning and modification of genes, construction of plasmids and purification of the recombinant proteins, amyloid-β, tau and α-synuclein. She investigates mechanisms of Parkinson's disease, in particular the interaction between α-synuclein, synaptic vesicles and calcium.  

Postdoctoral Researcher
Dr Amberley  Stephens

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