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Membrane-Accelerated Amyloid-? Aggregation and Formation of Cross-? Sheets.


ABSTRACT: Amyloid- ? aggregates play a causative role in Alzheimer's disease. These aggregates are a product of the physical environment provided by the basic neuronal membrane, composed of a lipid bilayer. The intrinsic properties of the lipid bilayer allow amyloid- ? peptides to nucleate and form well-ordered cross- ? sheets within the membrane. Here, we correlate the aggregation of the hydrophobic fragment of the amyloid- ? protein, A ? 25 - 35 , with the hydrophobicity, fluidity, and charge density of a lipid bilayer. We summarize recent biophysical studies of model membranes and relate these to the process of aggregation in physiological systems.

SUBMITTER: Khondker A 

PROVIDER: S-EPMC5618134 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

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Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets.

Khondker Adree A   Alsop Richard J RJ   Rheinstädter Maikel C MC  

Membranes 20170831 3


Amyloid- β aggregates play a causative role in Alzheimer's disease. These aggregates are a product of the physical environment provided by the basic neuronal membrane, composed of a lipid bilayer. The intrinsic properties of the lipid bilayer allow amyloid- β peptides to nucleate and form well-ordered cross- β sheets within the membrane. Here, we correlate the aggregation of the hydrophobic fragment of the amyloid- β protein, A β 25 - 35 , with the hydrophobicity, fluidity, and charge density of  ...[more]

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