Open Access. Powered by Scholars. Published by Universities.®
Social and Behavioral Sciences Commons™
Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 1 of 1
Full-Text Articles in Social and Behavioral Sciences
Amyloid-Β Oligomers Are Sequestered By Both Intracellular And Extracellular Chaperones, P Narayan, Sarah Meehan, John Carver, Mark Wilson, C M Dobson, D Klenerman
Amyloid-Β Oligomers Are Sequestered By Both Intracellular And Extracellular Chaperones, P Narayan, Sarah Meehan, John Carver, Mark Wilson, C M Dobson, D Klenerman
Mark R Wilson
The aberrant aggregation of the amyloid-β peptide into β-sheet rich, fibrillar structures proceeds via a heterogeneous ensemble of oligomeric intermediates that have been associated with neurotoxicity in Alzheimer’s disease (AD). Of particular interest in this context are the mechanisms by which molecular chaperones, part of the primary biological defenses against protein misfolding, influence Aβ aggregation. We have used single-molecule fluorescence techniques to compare the interactions between distinct aggregation states (monomers, oligomers, and amyloid fibrils) of the AD-associated amyloid-β(1–40) peptide, and two molecular chaperones, both of which are upregulated in the brains of patients with AD and have been found colocalized …