Chapter title |
Fluorescence Methods for Unraveling Oligomeric Amyloid Intermediates
|
---|---|
Chapter number | 10 |
Book title |
Protein Amyloid Aggregation
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-2978-8_10 |
Pubmed ID | |
Book ISBNs |
978-1-4939-2977-1, 978-1-4939-2978-8
|
Authors |
Niels Zijlstra, Nathalie Schilderink, Vinod Subramaniam |
Abstract |
Amyloid oligomers are considered to be the relevant toxic species in many amyloid diseases and much research effort has been devoted to fully characterize these oligomers. Despite their importance, oligomers have proven to be difficult to characterize structurally. Information on their aggregation number is scarce, largely because standard techniques struggle to provide reliable results. In this chapter, we present two different methods that reproducibly yield fluorescently labeled α-Synuclein oligomers. We then discuss a new approach, combining single-molecule photobleaching and sub-stoichiometric fluorescent labeling, that we have developed to determine the aggregation number of supramolecular protein assemblies. |
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