Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells

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The aberrant misfolding and subsequent conversion of monomeric protein into amyloid aggregates characterises many neurodegenerative disorders, including Parkinson's and Alzheimer's diseases. These aggregates are highly heterogeneous in structure, generally of low abundance and typically smaller than the diffraction limit of light (approximate to 250nm). To overcome the challenges these characteristics pose to the study of endogenous aggregates formed in cells, we have developed a method to characterise them at the nanometre scale without the need for a conjugated fluorophore. Using a combination of DNA PAINT and an amyloid-specific aptamer, we demonstrate that this technique is able to detect and super-resolve a range of aggregated species, including those formed by alpha-synuclein and amyloid-beta. Additionally, this method enables endogenous protein aggregates within cells to be characterised. We found that neuronal cells derived from patients with Parkinson's disease contain a larger number of protein aggregates than those from healthy controls.
Publisher
WILEY-V C H VERLAG GMBH
Issue Date
2018-10
Language
English
Article Type
Article
Citation

CHEMBIOCHEM, v.19, no.19, pp.2033 - 2038

ISSN
1439-4227
DOI
10.1002/cbic.201800209
URI
http://hdl.handle.net/10203/305027
Appears in Collection
BC-Journal Papers(저널논문)
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