Amyloid-beta membrane binding and permeabilization are distinct processes influenced separately by membrane charge and fluidity.

@article{Wong2009AmyloidbetaMB,
  title={Amyloid-beta membrane binding and permeabilization are distinct processes influenced separately by membrane charge and fluidity.},
  author={Pamela T Wong and Joseph A. Schauerte and Kathleen C. Wisser and Hao Ding and E Lyn Lee and Duncan G. Steel and Ari A Gafni},
  journal={Journal of molecular biology},
  year={2009},
  volume={386 1},
  pages={81-96}
}
The 40 and 42 residue amyloid-beta (Abeta) peptides are major components of the proteinaceous plaques prevalent in the Alzheimer's disease-afflicted brain and have been shown to have an important role in instigating neuronal degeneration. Whereas it was previously thought that Abeta becomes cytotoxic upon forming large fibrillar aggregates, recent studies suggest that soluble intermediate-sized oligomeric species cause cell death through membrane permeabilization. The present study examines the… CONTINUE READING

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