Unraveling the Early Events of Amyloid-β Protein (Aβ) Aggregation: Techniques for the Determination of Aβ Aggregate Size

International Journal of Molecular Sciences

N. Elizabeth Pryor¹  Melissa A. Moss² 

[1] Ralph E. Martin Department of Chemical Engineering, 3202 Bell Engineering Center, University of Arkansas, Fayetteville, AR 72701, USA; E-Mail:;Department of Chemical Engineering, 2C02 Swearingen Engineering Center, University of South Carolina, Columbia, SC 29208, USA; E-Mail:

关键词: amyloid;    capillary electrophoresis;    centrifugation;    fluorescence correlation spectroscopy;    light scattering;    mass spectrometry;    polyacrylamide gel electrophoresis;    oligomer;    size exclusion chromatography;    Western blotting;   

DOI  :  10.3390/ijms13033038

来源: mdpi

【 摘 要 】

The aggregation of proteins into insoluble amyloid fibrils coincides with the onset of numerous diseases. An array of techniques is available to study the different stages of the amyloid aggregation process. Recently, emphasis has been placed upon the analysis of oligomeric amyloid species, which have been hypothesized to play a key role in disease progression. This paper reviews techniques utilized to study aggregation of the amyloid-β protein (Aβ) associated with Alzheimer’s disease. In particular, the review focuses on techniques that provide information about the size or quantity of oligomeric Aβ species formed during the early stages of aggregation, including native-PAGE, SDS-PAGE, Western blotting, capillary electrophoresis, mass spectrometry, fluorescence correlation spectroscopy, light scattering, size exclusion chromatography, centrifugation, enzyme-linked immunosorbent assay, and dot blotting.

【 授权许可】

CC BY   
© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.