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

Journal

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 13, Issue 3, Pages 3038-3072

Publisher

MDPI
DOI: 10.3390/ijms13033038

Keywords

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

Funding

  1. National Center for Research Resources (NCRR) [1P30RR031154-02]
  2. National Institutes of Health (NIH)
  3. Arkansas Biosciences Institute

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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-beta protein (A beta) associated with Alzheimer's disease. In particular, the review focuses on techniques that provide information about the size or quantity of oligomeric A beta 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.

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