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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 A\u03b242. We show here that fluorinated and hydrogenated NPs with different abilities to change A\u03b242 conformation influence oligomerization as assessed by atomic force microscopy, immunoblot and SDS\u2010PAGE. Fluorinated NPs, which promote an increase in \u03b1\u2010helical 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 A\u03b242 into an \u03b1\u2010helical\u2010enriched secondary structure also has antiapoptotic activity, thereby increasing the viability of cells treated with oligomeric species.<\/jats:italic><\/jats:p>","DOI":"10.1002\/cbic.201000237","type":"journal-article","created":{"date-parts":[[2010,7,26]],"date-time":"2010-07-26T10:13:09Z","timestamp":1280139189000},"page":"1905-1913","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":40,"title":["Controlling Amyloid\u2010\u03b2 Peptide(1\u201342) Oligomerization and Toxicity by Fluorinated Nanoparticles"],"prefix":"10.1002","volume":"11","author":[{"given":"Ana M.","family":"Saraiva","sequence":"first","affiliation":[]},{"given":"Isabel","family":"Cardoso","sequence":"additional","affiliation":[]},{"given":"M. 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