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• W2896958434 abstract "The tyrosine based electrochemical analysis of the kinetics of Zn(II)-induced aggregation of the 42-amino-acid-long amyloid-β peptide (Aβ42) implicated in Alzheimer's disease pathogenesis was carried out by square wave voltammetry on carbon screen printed electrodes. As previously reported, the Aβ42 electrooxidation peak current can serve as an estimate of the fraction of Aβ42 peptide molecules not included in Zn(II)-induced Aβ42 aggregates/oligomers. The current was found to drop in a Zn(II)-dependent manner prior to the first measurement (in a minute after the addition of Zn(II) ions) but to remain unchanged during the following 30-min incubation period. The electrochemical analysis was applied in parallel with turbidimetry and dynamic light scattering (DLS) to monitor in time the occurrence of Aβ42 aggregates induced by substoichiometric Zn(II) concentrations. In contrast to the current, Aβ42 solution turbidity steadily increased with time in a Zn(II)-dependent manner during the 30-min incubation period. The turbidity increase was accompanied by the occurrence of large (micron-sized) Aβ42 aggregates detected by DLS. These findings suggest that the Zn(II)-induced aggregation of Aβ42 molecules proceeds via a two-stage mechanism which includes as the first step a fast formation of Aβ42 oligomers (large enough to effectively suppress the Aβ42 electrooxidation via a tyrosine residue), followed by the relatively slow assembly of these oligomers into bulky (micron-sized) aggregates. The Zn(II)-triggered Aβ42 oligomerization and, consequently, the overall Zn(II)-induced Aβ42 aggregation were found to depend on the solution ionic strength. When applied to N-truncated and phosphorylated Aβ42 isoforms, Aβ(6-42) and pS8-Aβ42, the combined analysis has revealed that their aggregation behavior differs from that of the Aβ42 peptide. While Zn(II)-triggered Aβ(6-42) oligomers demonstrated a higher propensity to assemble into micron-sized aggregates, compared to the Aβ42 peptide, Zn(II)-triggered pS8-Aβ42 oligomers lack the ability to form large aggregates. Thus, the direct electrochemistry when combined with methods allowing for detection of aggregates may provide deeper mechanistic insights into protein/peptide aggregation." @default.
• W2896958434 created "2018-10-26" @default.
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• W2896958434 date "2018-12-01" @default.
• W2896958434 modified "2023-10-17" @default.
• W2896958434 title "Electrochemical detection of Zn(II)-induced amyloid-β aggregation: Insights into aggregation mechanisms" @default.
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• W2896958434 doi "https://doi.org/10.1016/j.jelechem.2018.10.016" @default.
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