期刊
ACTA BIOCHIMICA POLONICA
卷 68, 期 2, 页码 169-179出版社
ACTA BIOCHIMICA POLONICA
DOI: 10.18388/abp.2020_5493
关键词
Alzheimer's disease; protein aggregation; metal-protein binding; neurodegeneration; pharmaceutics
资金
- Swedish Alzheimer Foundation
- Swedish Research Council
- Swedish Brain Foundation
- Magnus Bergvall Foundation
- Ulla-Carin Lindquist ALS Foundation
- Olle Engkvist's Foundation
- Stockholm Region
- Knut and Alice Wallenberg Foundation
Alzheimer's disease is a incurable disease and the main cause of age-related dementia worldwide. Research has shown promising results for the treatment of AD with lithium, although the underlying mechanism is still unclear. The interactions between A beta peptides and Li+ ions have not been well investigated in relation to AD pathology.
Alzheimer's disease (AD) is an incurable disease and the main cause of age-related dementia worldwide, despite decades of research. Treatment of AD with lithium (Li) has shown promising results, but the underlying mechanism is unclear. The pathological hallmark of AD brains is deposition of amyloid plaques, consisting mainly of amyloid-beta (A beta) peptides aggregated into amyloid fibrils. The plaques contain also metal ions of e.g. Cu, Fe, and Zn, and such ions are known to interact with A beta peptides and modulate their aggregation and toxicity. The interactions between A beta peptides and Li+ ions have however not been well investigated. Here, we use a range of biophysical techniques to characterize in vitro interactions between A beta peptides and Li+ ions. We show that Li+ ions display weak and non-specific interactions with A beta peptides, and have minor effects on A beta aggregation. These results indicate that possible beneficial effects of Li on AD pathology are not likely caused by direct interactions between A beta peptides and Li+ ions.
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