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Randomization of Amyloid‐β‐Peptide(1‐42) Conformation by Sulfonated and Sulfated Nanoparticles Reduces Aggregation and Cytotoxicity |
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| Authors: | Ana M. Saraiva Isabel Cardoso Maria João Saraiva Klaus Tauer M. Carmo Pereira Manuel A. N. Coelho Helmuth Möhwald Gerald Brezesinski |
| Affiliation: | 1. Max Planck Institute of Colloids and Interfaces, Wissenschaftspark Golm, 14476 Potsdam, Germany;2. LEPAE, Departamento de Engenharia Química, Faculdade de Engenharia da Universidade do Porto, Rua Dr. Roberto Frias, 4200‐465 Porto, Portugal;3. Molecular Neurobiology Unit, Instituto de Biologia Molecular e Celular, Rua do Campo Alegre 823, 4150‐180 Porto, Portugal;4. Escola Superior de Tecnologia da Saúde do Porto, Instituto Politécnico do Porto, Rua Valente Perfeito 322, 4400‐330 Vila Nova de Gaia, Portugal |
| 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.  |
| Keywords: | amyloid‐β peptides cytotoxicity nanoparticles oligomers polystyrene |