Aggregation of alpha-synuclein using single-molecule spectroscopy

The aggregation of alpha-synuclein (αS) protein from soluble monomer into solid amyloid fibrils in the brain is associated with a range of devastating neurodegenerative disorders such as Parkinson’s disease. Soluble oligomers formed during the aggregation process are highly neurotoxic and are thought to play a key role in the onset and spreading of disease. Despite their importance, these species are difficult to study by conventional experimental approaches owing to their transient nature, heterogeneity, low abundance and a remarkable sensitivity of the oligomerisation process to the chosen experimental conditions. In this thesis, well-established single-molecule techniques have been utilised to study the aggregation and oligomerisation of αS in solution.

Name dc:type.qualificationname

Doctor of Philosophy (PhD)

Level dc:type.qualificationlevel

Doctoral

Grantor dc:publisher.institution

University of Cambridge

Year dc:date.issued

2017

Author dc:creator

• Iljina, Marija

Advisor dc:contributor.advisor

• Klenerman, David

• alpha-synuclein
• single-molecule FRET
• protein aggregation
• neurodegeneration

Licence

• https://www.repository.cam.ac.uk/bitstreams/e70a814c-bb9d-4137-adf4-bb0af4ac63fb/download
• https://www.rioxx.net/licenses/all-rights-reserved/

Language dc:language

en

DOI dc:identifier.doi

https://doi.org/10.17863/CAM.8525

OAI identifier oai:identifier

oai:www.repository.cam.ac.uk:1810/263216