This title appears in the Scientific Report :
2018
Please use the identifier:
http://dx.doi.org/10.1039/C8CC02263A in citations.
Aβ under stress: the effects of acidosis, Cu 2+ -binding, and oxidation on amyloid β-peptide dimers
Aβ under stress: the effects of acidosis, Cu 2+ -binding, and oxidation on amyloid β-peptide dimers
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. Tran...
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Personal Name(s): | Liao, Qinghua |
---|---|
Owen, Michael C. / Bali, Sofia / Barz, Bogdan / Strodel, Birgit (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Chemical communications, 54 (2018) 56, S. 7766 - 7769 |
Imprint: |
Cambridge
Soc.
2018
|
PubMed ID: |
29947363 |
DOI: |
10.1039/C8CC02263A |
Document Type: |
Journal Article |
Research Program: |
Functional Macromolecules and Complexes |
Publikationsportal JuSER |
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. |