Molecular Neuroscience Group
Shining Light on Neurodegeneration
Intro
The Molecular Neuroscience Group focuses on investigating the molecular mechanisms that can cause neurodegenerative diseases, such as Parkinson’s disease (PD), Alzheimer's disease (AD), and Huntington’s disease (HD).
Many neurodegenerative diseases are caused by aberrant forms of proteins which tend to accumulate and aggregate into shapes, which are believed to be toxic to the brain cells of affected patients. The proteins thought to cause disease are referred to as amyloid proteins. Amyloids are special in that, under circumstances not yet fully understood, they can ‘misfold’ and in the ensuing misfolded states they have a tendency to clump together, and be ‘trafficked’ from one neuron to another in the brains of patients suffering from diseases such as PD, AD, and HD. In order to study these processes in live cells/organisms we use primary neuronal cultures, neuronal cell lines, and small organisms such as the earthworm C. elegans as models of disease.
Our research
α - synuclein
The protein α-synuclein (αSyn) is crucially involved in Parkinson’s Disease (PD). αSyn aggregation has been linked to early-onset familial forms of PD as well as to the sporadic late-onset forms. Normally, αSyn is a soluble, structurally disorganised protein, found in throughout the brain including in neuronal presynapses. In disease, however, αSyn becomes aggregated and forms highly structured insoluble fibrils that make up Lewy Bodies in patient brains. Although αSyn’s importance in PD has been recognised 20 years ago, the aetiology still remains largely unknown. We are therefore investigating both the normal physiological role of αSyn and the mechanisms that lead to aggregation and disease.
Amyloid β
Amyloid β is a 4 kD peptide formed by the sequential cleavage of the amyloid precursor protein. It ranges from 39-43 amino acids in length and exists primarily in two isoforms, Aβ40 and Aβ42. The normal physiological function of Aβ is not well understood, but the aggregation of Aβ42 is a pathological hallmark of Alzheimer’s disease, the most prevalent neurodegenerative disease affecting the elderly. Unraveling the molecular mechanisms through which peptide aggregation is initiated and proceeds is crucial for gaining a better understanding of the disease and designing new therapeutic strategies. Within our group, we have probed the mechanisms of Aβ aggregation using various in vitro and in vivo techniques
Tau
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.
Get in touch with us!
Cambridge University, Philippa Fawcett Dr, Cambridge CB3 0AS
tel: 123-456-7890
