Journal Article

FZJ-2018-07748

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Aβ under stress: the effects of acidosis, Cu 2+ -binding, and oxidation on amyloid β-peptide dimers

Liao, Q. ; Owen, M. C. ; Bali, S. ; Barz, B.FZJ* ; Strodel, B. (Corresponding author)FZJ*

2018
Soc. Cambridge

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Please use a persistent id in citations: doi:10.1039/C8CC02263A

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.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 551 - Functional Macromolecules and Complexes (POF3-551) (POF3-551)

Appears in the scientific report 2018

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Database coverage:
; Allianz-Lizenz / DFG ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; IF >= 5 ; JCR ; NCBI Molecular Biology Database ; National-Konsortium ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection

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