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

• Type: Article in International Scientific Journal
• Date: 2010

Authors

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

Journal

Title: Macromolecular Bioscience

Vol. 10

Pages: 1152-1163

ISSN: 1616-5187

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 22 Citations

Scopus - 15 Citations

Scientific classification

FOS: Engineering and technology > Materials engineering

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 12