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Metal binding to the amyloid-beta peptides in the presence of biomembranes: potential mechanisms of cell toxicity
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 82019 (English)In: Journal of Biological Inorganic Chemistry, ISSN 0949-8257, E-ISSN 1432-1327, Vol. 24, no 8, p. 1189-1196Article, review/survey (Refereed) Published
Abstract [en]

The amyloid-beta (A beta) peptides are key molecules in Alzheimer's disease (AD) pathology. They interact with cellular membranes, and can bind metal ions outside the membrane. Certain oligomeric A beta aggregates are known to induce membrane perturbations and the structure of these oligomers-and their membrane-perturbing effects-can be modulated by metal ion binding. If the bound metal ions are redox active, as e.g., Cu and Fe ions are, they will generate harmful reactive oxygen species (ROS) just outside the membrane surface. Thus, the membrane damage incurred by toxic A beta oligomers is likely aggravated when redox-active metal ions are present. The combined interactions between A beta oligomers, metal ions, and biomembranes may be responsible for at least some of the neuronal death in AD patients.

Place, publisher, year, edition, pages
2019. Vol. 24, no 8, p. 1189-1196
Keywords [en]
Amyloid-beta peptide, Phospholipid membrane, Redox-active metal ion, Cytotoxicity, Amyloid disease, Membrane pore, Reactive oxygen species
National Category
Biological Sciences Chemical Sciences
Identifiers
URN: urn:nbn:se:su:diva-177621DOI: 10.1007/s00775-019-01723-9ISI: 000501026900006PubMedID: 31562546OAI: oai:DiVA.org:su-177621DiVA, id: diva2:1384626
Available from: 2020-01-10 Created: 2020-01-10 Last updated: 2020-01-10Bibliographically approved

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Wärmländer, Sebastian K. T. S.Österlund, NicklasWallin, CeciliaJarvet, JüriGräslund, Astrid
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