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

被引：29
|
作者：
Saraiva, Ana M. [1 ,2 ]
Cardoso, Isabel [3 ,4 ]
Saraiva, Maria Joao [3 ]
Tauer, Klaus [1 ]
Pereira, M. Carmo [2 ]
Coelho, Manuel A. N. [2 ]
Moehwald, Helmuth [1 ]
Brezesinski, Gerald [1 ]
机构：
[1] Max Planck Inst Colloids & Interfaces, D-14476 Potsdam, Germany
[2] Univ Porto, LEPAE, Dept Engn Quim, Fac Engn, P-4200465 Oporto, Portugal
[3] Inst Biol Mol & Celular, Mol Neurobiol Unit, P-4150180 Oporto, Portugal
[4] Inst Politecn Porto, Escola Super Tecnol Saude Porto, P-4400330 Vila Nova De Gaia, Portugal
来源：
MACROMOLECULAR BIOSCIENCE | 2010年 / 10卷 / 10期
关键词：
amyloid-beta peptides; cytotoxicity; nanoparticles; oligomers; polystyrene; SMALL-MOLECULE INHIBITORS; CENTRAL-NERVOUS-SYSTEM; BETA-AMYLOID PEPTIDES; PROTEIN A-BETA; ALZHEIMERS-DISEASE; TEMPERATURE-DEPENDENCE; OLIGOMERS; NEUROTOXICITY; DEGENERATION; A-BETA(1-42);
D O I：
10.1002/mabi.200900448
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：1152 / 1163
页数：12
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