1. Metal binding to the amyloid-β peptides in the presence of biomembranes: potential mechanisms of cell toxicity
- Author
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Jüri Jarvet, Astrid Gräslund, Nicklas Österlund, Ann Tiiman, Cecilia Wallin, Jinghui Luo, Jinming Wu, and Sebastian K.T.S. Wärmländer
- Subjects
0301 basic medicine ,Iron ,Metal ions in aqueous solution ,Biochemistry ,Inorganic Chemistry ,Metal ,03 medical and health sciences ,Amyloid disease ,0302 clinical medicine ,Alzheimer Disease ,Humans ,Molecule ,Amino Acid Sequence ,Cytotoxicity ,chemistry.chemical_classification ,Reactive oxygen species ,Amyloid beta-Peptides ,Chemistry ,Cell Membrane ,Amyloid β peptide ,030104 developmental biology ,Membrane ,visual_art ,Biophysics ,visual_art.visual_art_medium ,Reactive Oxygen Species ,Copper ,030217 neurology & neurosurgery ,Protein Binding - Abstract
The amyloid-β (Aβ) 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 Aβ 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 Aβ oligomers is likely aggravated when redox-active metal ions are present. The combined interactions between Aβ oligomers, metal ions, and biomembranes may be responsible for at least some of the neuronal death in AD patients.
- Published
- 2019
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