The delaying effect of oxAβ on metal altered Aβ assembly was also observed. ![]() In the presence of copper or zinc di-cations, oxAβ assembled into weakly-structured aggregates rather than short, untangled Cu-Aβ fibrils and long untangled Zn-Aβ fibrils. However, oxAβ does not change the quantity and morphology of the Aβ fibrils formed to a significant extent. In a mixture of the two peptides, oxAβ has a mainly kinetic effect on the assembly of the Aβ peptide and was able to slow down the formation of Aβ fibril in a wide pH range. In addition, oxAβ does affect the assembly of the parent Aβ peptide. ![]() oxAβ was still able to assemble but displayed ill-defined and small oligomeric assemblies compared to the long and thick β-sheet rich fibrils from the non-oxidized counterpart. To accomplish this, we performed kinetics and analysis on an oxidized Aβ ( oxAβ) peptide, resulting from the attack of reactive oxygen species (ROS) that are formed by the biologically relevant Cu/Aβ/dioxygen/ascorbate system. ![]() The present study aims at investigating the fallouts of Aβ oxidation on the assembly properties of the Aβ peptide. Oxidative stress that can lead to oxidation of the amyloid-β (Aβ) peptide is considered a key feature in Alzheimer’s disease (AD), influencing the ability of Aβ to assemble into β-sheet rich fibrils that are commonly found in senile plaques of AD patients.
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