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ABSTRACT: Background
Protein aggregation plays a major role in the pathogenesis of neurodegenerative disorders, such as Alzheimer's disease. However, direct real-time imaging of protein aggregation, including oligomerization and fibrillization, has never been achieved. Here we demonstrate the preparation of fluorescent semiconductor nanocrystal (quantum dot; QD)-labeled amyloid-beta peptide (QDAbeta) and its advanced applications.Methodology/principal findings
The QDAbeta construct retained Abeta oligomer-forming ability, and the sizes of these oligomers could be estimated from the relative fluorescence intensities of the imaged spots. Both QDAbeta coaggregation with intact Abeta42 and insertion into fibrils were detected by fluorescence microscopy. The coaggregation process was obse
SUBMITTER: Tokuraku K
PROVIDER: S-EPMC2794548 | biostudies-literature | 2009 Dec
REPOSITORIES: biostudies-literature