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Controlling Amyloid‐β Peptide(1–42) Oligomerization and Toxicity by Fluorinated Nanoparticles
Author(s) -
Saraiva Ana M.,
Cardoso Isabel,
Pereira M. Carmo,
Coelho Manuel A. N.,
Saraiva Maria João,
Möhwald Helmuth,
Brezesinski Gerald
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000237
Subject(s) - cytotoxicity , fibril , peptide , neurodegeneration , chemistry , senile plaques , biophysics , amyloid (mycology) , amyloid beta , biochemistry , neurotoxicity , alzheimer's disease , microbiology and biotechnology , toxicity , in vitro , biology , disease , medicine , organic chemistry , inorganic chemistry , pathology
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.