Open AccessLithium ions display weak interaction with amyloid-beta (Aβ) peptides and have minor effects on their aggregation
Author(s) -
Elina Berntsson,
Suman Paul,
Faraz Vosough,
Sabrina B. Sholts,
Jüri Jarvet,
Per M. Roos,
Andreas Barth,
Astrid Gräslund,
Sebastian K.T.S. Wärmländer
Publication year - 2021
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.2020_5493
Subject(s) - chemistry , biophysics , fibril , peptide , amyloid (mycology) , lithium (medication) , ion , metal ions in aqueous solution , in vitro , biochemistry , biology , medicine , inorganic chemistry , organic chemistry
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 showed promising results, but the underlying mechanism is unclear. The pathological hallmark of AD brains is deposition of amyloid plaques, consisting mainly of amyloid-β (Aβ) 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 Aβ peptides and modulate their aggregation and toxicity. The interactions between Aβ peptides and Li+ ions have however not been well investigated. Here, we use a range of biophysical techniques to characterize in vitro interactions between Aβ peptides and Li+ ions. We show that Li+ ions display weak and non-specific interactions with Aβ peptides, and have minor effects on Aβ aggregation. These results indicate that possible beneficial effects of Li on AD pathology are not likely caused by direct interactions between Aβ peptides and Li+ ions.