Randomization of Amyloid-beta-Peptide(1-42) Conformation by Sulfonated and Sulfated Nanoparticles Reduces Aggregation and Cytotoxicity

• Tipo: Artigo em Revista Científica Internacional
• Data: 2010

Autores

Ana M Saraiva (Autor) Outra; Isabel Cardoso (Autor) Outra; Maria Joao Saraiva (Autor) ICBAS; Klaus Tauer (Autor) Outra; Carmo C Pereira (Autor) FEUP; Manuel A N Coelho (Autor) FEUP; Helmuth Moehwald (Autor) Outra; Gerald Brezesinski (Autor) Outra

Revista

Título: Macromolecular Bioscience

Vol. 10

Páginas: 1152-1163

ISSN: 1616-5187

Editora: Wiley-Blackwell

Indexação

ISI Web of Knowledge - 22 Citações

Scopus - 15 Citações

Classificação Científica

FOS: Ciências da engenharia e tecnologias > Engenharia dos materiais

Outras Informações

ID Authenticus: P-003-1Y5

DOI: 10.1002/mabi.200900448

Abstract (EN): The amyloid-beta peptide (A beta) plays a central role in the mechanism of Alzheimer's disease, being the main constituent of the plaque deposits found in AD brains. A beta amyloid formation and deposition are due to a conformational switching to a beta-enriched secondary structure. Our strategy to inhibit A beta aggregation involves the reconversion of A beta 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 AB 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 12