Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids.
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ABSTRACT: The misfolding and aggregation of proteins into amyloid fibrils characterizes many neurodegenerative disorders such as Parkinson's and Alzheimer's diseases. We report here a method, termed SAVE (single aggregate visualization by enhancement) imaging, for the ultrasensitive detection of individual amyloid fibrils and oligomers using single-molecule fluorescence microscopy. We demonstrate that this method is able to detect the presence of amyloid aggregates of α-synuclein, tau, and amyloid-β. In addition, we show that aggregates can also be identified in human cerebrospinal fluid (CSF). Significantly, we see a twofold increase in the average aggregate concentration in CSF from Parkinson's disease patients compared to age-matched controls. Taken together, we conclude that this method provides
SUBMITTER: Horrocks MH
PROVIDER: S-EPMC4800427 | biostudies-literature | 2016 Mar
REPOSITORIES: biostudies-literature
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