Randomization of amyloid-β-peptide(1-42) conformation by sulfonated and sulfated nanoparticles reduces aggregation and cytotoxicity.

Abstract:

:The amyloid-β peptide (Aβ) plays a central role in the mechanism of Alzheimer's disease, being the main constituent of the plaque deposits found in AD brains. Aβ amyloid formation and deposition are due to a conformational switching to a β-enriched secondary structure. Our strategy to inhibit Aβ aggregation involves the re-conversion of Aβ conformation by adsorption to nanoparticles. NPs were synthesized by sulfonation and sulfation of polystyrene, leading to microgels and latexes. Both polymeric nanostructures affect the conformation of Aβ inducing an unordered state. Oligomerization was delayed and cytotoxicity reduced. The proper balance between hydrophilic moieties and hydrophobic chains seems to be an essential feature of effective NPs.

journal_name

Macromol Biosci

authors

Saraiva AM,Cardoso I,Saraiva MJ,Tauer K,Pereira MC,Coelho MA,Möhwald H,Brezesinski G

doi

10.1002/mabi.200900448

subject

Has Abstract

pub_date

2010-10-08 00:00:00

pages

1152-63

issue

10

eissn

1616-5187

issn

1616-5195

journal_volume

10

pub_type

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