Randomization of amyloid-ß-peptide(1-42) conformation by sulfonated and sulfated nanoparticles reduces aggregation and cytotoxicity.
Macromol Biosci
; 10(10): 1152-63, 2010 Oct 08.
Article
em En
| MEDLINE
| ID: mdl-20480510
ABSTRACT
The amyloid-ß peptide (Aß) plays a central role in the mechanism of Alzheimer's disease, being the main constituent of the plaque deposits found in AD brains. Aß amyloid formation and deposition are due to a conformational switching to a ß-enriched secondary structure. Our strategy to inhibit Aß aggregation involves the re-conversion of Aß 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 Aß 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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Conformação Proteica
/
Peptídeos beta-Amiloides
/
Nanopartículas
Tipo de estudo:
Clinical_trials
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Macromol Biosci
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2010
Tipo de documento:
Article
País de afiliação:
Alemanha
País de publicação:
ALEMANHA
/
ALEMANIA
/
DE
/
DEUSTCHLAND
/
GERMANY