Dual Effect of Amino Modified Polystyrene Nanoparticles on Amyloid β Protein Fibrillation

被引:236
作者
Cabaleiro-Lago, Celia [1 ]
Quinlan-Pluck, Fiona [1 ]
Lynch, Iseult [1 ]
Dawson, Kenneth A. [1 ]
Linse, Sara [2 ]
机构
[1] Natl Univ Ireland Univ Coll Dublin, Sch Chem & Chem Biol, Ctr BioNano Interact, Dublin 4, Ireland
[2] Lund Univ, Dept Biochem, S-22100 Lund, Sweden
来源
ACS CHEMICAL NEUROSCIENCE | 2010年 / 1卷 / 04期
基金
瑞典研究理事会; 爱尔兰科学基金会;
关键词
Amyloid; aggregation kinetics; nanoparticles; ALZHEIMERS-DISEASE; AGGREGATION; NUCLEATION; INHIBITION; KINETICS;
D O I
10.1021/cn900027u
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 fibrillation kinetics of the amyloid beta peptide is analyzed in presence of cationic polystyrene nanoparticles of different size. The results highlight the importance of the ratio between the peptide and particle concentration. Depending on the specific ratio, the kinetic effects vary from acceleration of the fibrillation process by reducing the lag phase at low particle surface area in solution to inhibition of the fibrillation process at high particle surface area. The kinetic behavior can be explained if we assume a balance between two different pathways: first fibrillation of free monomer in solution and second nucleation and fibrillation promoted at the particle surface. The overall rate of fibrillation will depend on the interplay between these two pathways, and the predominance of one mechanism over the other will be determined by the relative equilibrium and rate constants.
引用
收藏
页码:279 / 287
页数:9
相关论文
共 24 条
[1]   Aggregation and catabolism of disease-associated intra-Aβ mutations:: reduced proteolysis of AβA21G by neprilysin [J].
Betts, Vicki ;
Leissring, Malcolm A. ;
Dolios, Georgia ;
Wang, Rong ;
Selkoe, Dennis J. ;
Walsh, Dominic M. .
NEUROBIOLOGY OF DISEASE, 2008, 31 (03) :442-450
[2]   Inhibition of IAPP and IAPP(20-29) Fibrillation by Polymeric Nanoparticles [J].
Cabaleiro-Lago, C. ;
Lynch, I. ;
Dawson, K. A. ;
Linse, S. .
LANGMUIR, 2010, 26 (05) :3453-3461
[3]   Inhibition of Amyloid β Protein Fibrillation by Polymeric Nanoparticles [J].
Cabaleiro-Lago, Celia ;
Quinlan-Pluck, Fiona ;
Lynch, Iseult ;
Lindman, Stina ;
Minogue, Aedin M. ;
Thulin, Eva ;
Walsh, Dominic M. ;
Dawson, Kenneth A. ;
Linse, Sara .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2008, 130 (46) :15437-15443
[4]   Protein misfolding, functional amyloid, and human disease [J].
Chiti, Fabrizio ;
Dobson, Christopher M. .
ANNUAL REVIEW OF BIOCHEMISTRY, 2006, 75 :333-366
[5]  
Ferrone F, 1999, METHOD ENZYMOL, V309, P256
[6]   Conformational changes of the amyloid β-peptide (1-40) adsorbed on solid surfaces [J].
Giacomelli, CE ;
Norde, W .
MACROMOLECULAR BIOSCIENCE, 2005, 5 (05) :401-407
[7]  
GIEHM L, J MOL BIOL UNPUB
[8]   Medicine - The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics [J].
Hardy, J ;
Selkoe, DJ .
SCIENCE, 2002, 297 (5580) :353-356
[9]   Amyloid β-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process [J].
Hellstrand, Erik ;
Boland, Barry ;
Walsh, Dominic M. ;
Linse, Sara .
ACS CHEMICAL NEUROSCIENCE, 2010, 1 (01) :13-18
[10]   Inhibition of toxicity in the β-amyloid peptide fragment β-(25-35) using N-methylated derivatives -: A general strategy to prevent amyloid formation [J].
Hughes, E ;
Burke, RM ;
Doig, AJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (33) :25109-25115