Gold Nanoparticles as a Probe for Amyloid-β Oligomer and Amyloid Formation

被引:49
|
作者
Elbassal, Esmail A. [1 ]
Morris, Clifford [1 ]
Kent, Thomas W. [1 ]
Lantz, Richard [1 ]
Ojha, Bimlesh [1 ]
Wojcilciewicz, Ewa P. [2 ]
Du, Deguo [1 ]
机构
[1] Florida Atlantic Univ, Charles E Schmidt Coll Med, Dept Chem & Biochem, Boca Raton, FL 33431 USA
[2] Florida Atlantic Univ, Charles E Schmidt Coll Med, Dept Biomed Sci, Boca Raton, FL 33431 USA
来源
JOURNAL OF PHYSICAL CHEMISTRY C | 2017年 / 121卷 / 36期
基金
美国国家卫生研究院;
关键词
ALZHEIMERS-DISEASE; COLORIMETRIC DETECTION; OPTICAL-PROPERTIES; A-BETA; ELECTROSTATIC INTERACTIONS; PROTEIN FIBRILLATION; SILVER NANOPARTICLES; CEREBROSPINAL-FLUID; NUCLEATION; HYPOTHESIS;
D O I
10.1021/acs.jpcc.7b05169
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The process of amyloid-beta (A beta) amyloid formation is pathologically linked to Alzheimer's disease (AD). The identification of A beta amyloids and intermediates that are crucial players in the pathology of AD is critical for exploring the underlying mechanism of A beta aggregation and the diagnosis of the disease. Herein, we performed a gold nanoparticle (AuNP)-based study to detect the formation of A beta amyloid fibrils and oligomers. Our results demonstrate that the intensity of the surface plasmon resonance (SPR) absorption band of the AuNPs is sensitive to the quantity of A beta 40 amyloids. This allows the SPR assay to be used for detection and semiquantification of A beta 40 amyloids and characterization of the kinetics of A beta amyloid formation. Furthermore, our study demonstrates that the SPR band intensity of the AuNPs is sensitive to the presence of oligomers of A beta 40, and an A,840 mutant which forms more stable oligomers. The kinetics of the stable oligomer formation of the A beta 40 mutant can also be monitored following the SPR band intensity change of AuNPs. Our results indicate that this nanoparticle-based method can be used for mechanistic studies of early protein self-assembly and fibrillogenesis.
引用
收藏
页码:20007 / 20015
页数:9
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