| Autor: |
Liao, Qinghua, Owen, Michael C., Bali, Sofia, Barz, Bogdan, Strodel, Birgit |
| Předmět: |
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| Zdroj: |
Chemical Communications; 7/18/2018, Vol. 54 Issue 56, p7766-7769, 4p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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