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Issue 56, 2018
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Aβ under stress: the effects of acidosis, Cu2+-binding, and oxidation on amyloid β-peptide dimers

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Abstract

In light of the high affinity of Cu2+ for Alzheimer's Aβ1–42 and its ability to subsequently catalyze the formation of radicals, we examine the effects of Cu2+ binding, Aβ oxidation, and an acidic environment on the conformational dynamics of the smallest Aβ1–42 oligomer, the Aβ1–42 dimer. Transition networks calculated from Hamiltonian replica exchange molecular dynamics (H-REMD) simulations reveal that the decreased pH considerably increased the β-sheet content, whereas Cu2+ binding increased the exposed hydrophobic surface area, both of which can contribute to an increased oligomerization propensity and toxicity.

Graphical abstract: Aβ under stress: the effects of acidosis, Cu2+-binding, and oxidation on amyloid β-peptide dimers

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Publication details

The article was received on 21 Mar 2018, accepted on 11 Jun 2018 and first published on 18 Jun 2018


Article type: Communication
DOI: 10.1039/C8CC02263A
Chem. Commun., 2018,54, 7766-7769

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    Aβ under stress: the effects of acidosis, Cu2+-binding, and oxidation on amyloid β-peptide dimers

    Q. Liao, M. C. Owen, S. Bali, B. Barz and B. Strodel, Chem. Commun., 2018, 54, 7766
    DOI: 10.1039/C8CC02263A

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