Internal and environmental effects on folding and dimerisation of Alzheimer's β-amyloid peptide

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Amyloid deposits are a hallmark of many diseases. In the case of Alzheimer's disease, a turn between 21Ala and 30Ala, stabilised by a salt bridge between 22Glu/23Asp and 28Lys, may nucleate folding and aggregation of the amyloid β(Aβ) peptide. In the present paper, we test this hypothesis by studying how salt bridge and turn formation vary with intrinsic and environmental changes, and how these changes affect folding and aggregation of the Aβ-peptide. © 2011 Taylor & Francis.

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Molecular Simulation