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
相关论文
共 50 条
  • [1] Investigating amyloid-β oligomer and fibril dynamics using a novel amyloid-β oligomer-specific antibody
    Silverman, Judith M.
    Gibbs, Ebrima
    Cowan, Catherine M.
    Cashman, Neil R.
    PRION, 2015, 9 : S43 - S43
  • [2] Mechanisms of Amyloid-β 42 oligomer formation from kinetic analysis
    Michaels, T. C.
    Saric, A.
    Lazell, H. W.
    Arosio, P.
    Vendruscolo, M.
    Dobson, C. M.
    Linse, S.
    Knowles, T. P. J.
    EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 2017, 46 : S240 - S240
  • [3] Amyloid-β Aggregation with Gold Nanoparticles on Brain Lipid Bilayer
    Lee, Hyojin
    Kim, Yuna
    Park, Anna
    Nam, Jwa-Min
    SMALL, 2014, 10 (09) : 1779 - 1789
  • [4] Taxifolin inhibits amyloid-β oligomer formation and fully restores vascular integrity and memory in cerebral amyloid angiopathy
    Saito, S.
    Yamamoto, Y.
    Maki, T.
    Fukushima, M.
    Takahashi, R.
    Ihara, M.
    JOURNAL OF THE NEUROLOGICAL SCIENCES, 2017, 381 : 988 - 988
  • [5] Taxifolin inhibits amyloid-β oligomer formation and fully restores vascular integrity and memory in cerebral amyloid angiopathy
    Satoshi Saito
    Yumi Yamamoto
    Takakuni Maki
    Yorito Hattori
    Hideki Ito
    Katsuhiko Mizuno
    Mariko Harada-Shiba
    Raj N. Kalaria
    Masanori Fukushima
    Ryosuke Takahashi
    Masafumi Ihara
    Acta Neuropathologica Communications, 5
  • [6] Taxifolin inhibits amyloid-β oligomer formation and fully restores vascular integrity and memory in cerebral amyloid angiopathy
    Saito, Satoshi
    Yamamoto, Yumi
    Maki, Takakuni
    Hattori, Yorito
    Ito, Hideki
    Mizuno, Katsuhiko
    Harada-Shiba, Mariko
    Kalaria, Raj N.
    Fukushima, Masanori
    Takahashi, Ryosuke
    Ihara, Masafumi
    ACTA NEUROPATHOLOGICA COMMUNICATIONS, 2017, 5 : 26
  • [7] Monomeric amyloid-β reduced amyloid-β oligomer-induced synapse damage in neuronal cultures
    Bate, Clive
    Williams, Alun
    NEUROBIOLOGY OF DISEASE, 2018, 111 : 48 - 58
  • [8] Pathways of Amyloid-β Aggregation Depend on Oligomer Shape
    Barz, Bogdan
    Liao, Qinghua
    Strodel, Birgit
    JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2018, 140 (01) : 319 - 327
  • [9] Pathways of Amyloid-β Aggregation Depend on Oligomer Shape
    Barz, Bogdan (b.barz@fz-juelich.de), 1600, American Chemical Society (140):
  • [10] The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade
    Cline, Erika N.
    Bicca, Maira Assuncao
    Viola, Kirsten L.
    Klein, William L.
    JOURNAL OF ALZHEIMERS DISEASE, 2018, 64 : S567 - S610