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| 001 | 843873 | ||
| 005 | 20210129232710.0 | ||
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| 100 | 1 | _ | |a Zhang, Tao |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Stoichiometric Zn 2+ interferes with the self-association of Aβ42: Insights from size distribution analysis |
| 260 | _ | _ | |a New York, NY [u.a.] |c 2018 |b Elsevier |
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| 520 | _ | _ | |a The abnormal aggregation of amyloid β (Aβ) peptides in the brain has been recognized as a central event in Alzheimer's disease (AD). Divalent metal ions such as Zn2+ have been shown to be closely involved in modulating Aβ self-association. Although the link between Zn2+ dyshomeostasis and brain Aβ deposition has been established, the effect of Zn2+ on the aggregation of Aβ is still incompletely clarified. By combining analytical ultracentrifugation (AUC), circular dichroism (CD) spectroscopy, thioflavin T (ThT) assay and atomic force microscopy (AFM) imaging, we analyzed the impact of stoichiometric Zn2+ on the aggregation process of Aβ42, the main toxic isoform of Aβ species in the brain. Aβ42 aggregates found in the presence of Zn2+ were smaller in size, non-fibrillary and showed less β-sheet structures than aggregates formed in absence of Zn2+. AUC showed that Zn2+ was capable of retaining monomeric Aβ42 in solution. Zn2+ chelation by EDTA totally reversed the inhibitory effect of Zn2+ on Aβ42 fibrillation. Our results provide further evidence that Zn2+ shifts the self-association of Aβ42 toward a non-fibrillary pathway by interfering with the aggregation process at multiple levels. |
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| 700 | 1 | _ | |a Pauly, Thomas |0 0000-0001-6556-7145 |b 1 |
| 700 | 1 | _ | |a Nagel-Steger, Luitgard |0 P:(DE-Juel1)162443 |b 2 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.ijbiomac.2018.02.123 |g p. S0141813017348365 |0 PERI:(DE-600)1483284-7 |p 631-639 |t International journal of biological macromolecules |v 113 |y 2018 |x 0141-8130 |
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