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Binding of the Molecular Chaperone αB-Crystallin to Aβ Amyloid Fibrils Inhibits Fibril Elongation

Shammas, Sarah L.; Waudby, Christopher A.; Wang, Shuyu; Buell, Alexander K.; Knowles, Tuomas P.J.; Ecroyd, Heath; Welland, Mark E.; Carver, John A.; Dobson, Christopher M.; Meehan, Sarah


The molecular chaperone αB-crystallin is a small heat-shock protein that is upregulated in response to a multitude of stress stimuli, and is found colocalized with Aβ amyloid fibrils in the extracellular plaques that are characteristic of Alzheimer's disease. We investigated whether this archetypical small heat-shock protein has the ability to interact with Aβ fibrils in vitro. We find that αB-crystallin binds to wild-type Aβ(42) fibrils with micromolar affinity, and also binds to fibrils...[Show more]

CollectionsANU Research Publications
Date published: 2011
Type: Journal article
Source: Biophysical Journal
DOI: 10.1016/j.bpj.2011.07.056
Access Rights: Open Access


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