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Aβ(M1-40) and Wild-Type Aβ40 Self-Assemble into Oligomers with Distinct Quaternary Structures.
Jacob L Bouchard1, Taylor C Davey2, Todd M Doran3,4
1Department of Medicinal Chemistry, University of Minnesota, Minneapolis, MN 55455, USA. bouch171@umn.edu.
Molecules (Basel, Switzerland)
|June 19, 2019
Summary
Researchers developed a new assay to study amyloid-beta oligomers (AβOs), crucial in Alzheimer's disease (AD). This method reveals diverse AβO structures, aiding the search for toxic species causing synaptic dysfunction.
Area of Science:
- Neuroscience
- Biochemistry
- Molecular Biology
Background:
- Amyloid-beta oligomers (AβOs) are implicated in Alzheimer's disease (AD) pathogenesis.
- The structure-function relationship of AβOs is critical for understanding synaptotoxicity but is difficult to study in vivo due to their low abundance and sensitivity.
Purpose of the Study:
- To develop a biochemical assay for quantifying the relative abundance and morphology of cross-linked AβOs.
- To compare oligomers derived from synthetic Aβ40 and a recombinant source (Aβ(M1-40)).
- To identify self-assembly conditions stabilizing specific AβO quaternary structures.
Main Methods:
- Development of a simple biochemical assay for cross-linked AβOs.
- Comparison of oligomers from wild-type Aβ40 and Aβ(M1-40) using the assay.
- Characterization of oligomer size, dispersity, and morphology.
Main Results:
- Both synthetic Aβ40 and Aβ(M1-40) formed oligomers with common sizes and morphology.
- Aβ(M1-40) oligomers exhibited greater diversity in quaternary structure, dispersity, and morphology.
- Self-assembly conditions were identified to stabilize high-molecular weight Aβ(M1-40) oligomers (>36 kDa).
Conclusions:
- The developed assay facilitates the study of AβO quaternary structure and morphology.
- Diverse quaternary structures of Aβ(M1-40) oligomers were characterized.
- This research is expected to aid in isolating toxic AβO species contributing to synaptic dysfunction in Alzheimer's disease.
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