Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
University of Cambridge · Bridge University · +1 more institution
Abstract
Protein aggregation is a complex process resulting in the formation of heterogeneous mixtures of aggregate populations that are closely linked to neurodegenerative conditions, such as Alzheimer's disease. Here, we find that soluble aggregates formed at different stages of the aggregation process of amyloid beta (Aβ42) induce the disruption of lipid bilayers and an inflammatory response to different extents. Further, by using gradient ultracentrifugation assay, we show that the smaller aggregates are those most potent at inducing membrane permeability and most effectively inhibited by antibodies binding to the C-terminal region of Aβ42. By contrast, we find that the larger soluble aggregates are those most…
Citation impact
- FWCI
- 46.66
- Percentile
- 100%
- References
- 53
Authors
17Topics & keywords
- Chemistry
- Protein aggregation
- Microglia
- Ultracentrifuge
- Antibody
- Biophysics
- Amyloid (mycology)
- Toxicity