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Protein misfolding and aggregation into structures like oligomers and fibrils are linked to various neurodegenerative diseases.
Traditional methods for studying these aggregates often lack specificity and rely on labeled proteins or non-specific stains.
The researchers developed a new technique using a high-affinity antibody with unique fluorophores and advanced microscopy to specifically identify and analyze α-synuclein aggregates in low concentrations, relevant to biological samples.
Article Abstract
Protein misfolding and aggregation into oligomeric and fibrillar structures is a common feature of many neurogenerative disorders. Single-molecule techniques have enabled characterization of these lowly abundant, highly heterogeneous protein aggregates, previously inaccessible using ensemble averaging techniques. However, they usually rely on the use of recombinantly-expressed labeled protein, or on the addition of amyloid stains that are not protein-specific. To circumvent these challenges, we have made use of a high affinity antibody labeled with orthogonal fluorophores combined with fast-flow microfluidics and single-molecule confocal microscopy to specifically detect α-synuclein, the protein associated with Parkinson's disease. We used this approach to determine the number and size of α-synuclein aggregates down to picomolar concentrations in biologically relevant samples.
