Oligomerisation of Parkinson's Alpha Synuclein - Smith, Rachel
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The extracellular deposition of misfolded protein aggregates, known as amyloid plaques, is associated with a variety of neurodegenerative disorders such as Alzheimer's, Parkinson's and Prion diseases. However, a poor correlation between amyloid aggregation and disease pathogenesis has led to the proposal of the existence of an intermediate oligomeric toxic species. Alpha-synuclein is the major component of Lewy body plaques observed in Parkinson's disease. Studies of -synuclein oligomers have proven difficult as the preparation of homogeneous, oligomeric -synuclein is problematic, due to the…mehr

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Produktbeschreibung
The extracellular deposition of misfolded protein aggregates, known as amyloid plaques, is associated with a variety of neurodegenerative disorders such as Alzheimer's, Parkinson's and Prion diseases. However, a poor correlation between amyloid aggregation and disease pathogenesis has led to the proposal of the existence of an intermediate oligomeric toxic species. Alpha-synuclein is the major component of Lewy body plaques observed in Parkinson's disease. Studies of -synuclein oligomers have proven difficult as the preparation of homogeneous, oligomeric -synuclein is problematic, due to the complexity of protein misfolding and aggregation. Here, two competing protocols for oligomer generation are compared in parallel to additional conditions, with the aim of identifying optimal requirements for oligomer formation.
Autorenporträt
Rachel graduated from the University of Warwick with a first class BSc degree in Biochemistry before moving into a career in clinical research. Rachel was first inspired by neurodegenerative disease research whilst studying at Warwick and her passion in this area has strengthened following personal experiences with dementia in her family.