Format:
Online-Ressource
ISSN:
1439-7633
Content:
Abstract: The amyloid‐β peptide (Aβ) is a major fibrillar component of neuritic plaques in Alzheimer's disease brains and is related to the pathogenesis of the disease. Soluble oligomers that precede fibril formation have been proposed as the main neurotoxic species that contributes to neurodegeneration and dementia. We hypothesize that oligomerization and cytotoxicity can be repressed by nanoparticles (NPs) that induce conformational changes in Aβ42. We show here that fluorinated and hydrogenated NPs with different abilities to change Aβ42 conformation influence oligomerization as assessed by atomic force microscopy, immunoblot and SDS‐PAGE. Fluorinated NPs, which promote an increase in α‐helical content, exert an antioligomeric effect, whereas hydrogenated analogues do not and lead to aggregation. Cytotoxicity assays confirmed our hypothesis by indicating that the conformational conversion of Aβ42 into an α‐helical‐enriched secondary structure also has antiapoptotic activity, thereby increasing the viability of cells treated with oligomeric species.
In:
volume:11
In:
number:13
In:
year:2010
In:
pages:1905-1913
In:
extent:9
In:
ChemBioChem, Weinheim : Wiley-VCH, [2000]-, 11, Heft 13 (2010), 1905-1913 (gesamt 9), 1439-7633
Language:
English
DOI:
10.1002/cbic.201000237
URN:
urn:nbn:de:101:1-2023042708551199617325
URL:
https://doi.org/10.1002/cbic.201000237
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2023042708551199617325
URL:
https://d-nb.info/1287152775/34
URL:
https://doi.org/10.1002/cbic.201000237
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