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Updated: Jun 13, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
Randomization of amyloid-β-peptide(1-42) conformation by sulfonated and sulfated nanoparticles reduces aggregation
Ana M Saraiva1, Isabel Cardoso, Maria João Saraiva
1Max Planck Institute of Colloids and Interfaces, Wissenschaftspark Golm, Potsdam, Germany. saraiva@mpikg.mpg.de
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.
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