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Chem Soc Rev. 2014 Oct 7;43(19):6692-700. doi: 10.1039/c3cs60431d.

Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.

Author information

1
Biophysics and Department of Chemistry, University of Michigan, 930 N. University Ave, Ann Arbor, MI 48109-1055, USA. ramamoor@umich.edu.

Abstract

The association of the amyloid-β (Aβ) peptide with cellular membranes is hypothesized to be the underlying phenomenon of neurotoxicity in Alzheimer's disease. Misfolding of proteins and peptides, as is the case with Aβ, follows a progression from a monomeric state, through intermediates, ending at long, unbranched amyloid fibers. This tutorial review offers a perspective on the association of toxic Aβ structures with membranes as well as details of membrane-associated mechanisms of toxicity.

PMID:
24464312
PMCID:
PMC4110197
DOI:
10.1039/c3cs60431d
[Indexed for MEDLINE]
Free PMC Article

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