Abstract
β-Amyloid protein (Aβ) is the major component of senile plaques found in the brains of Alzheimer's patients. A novel ELISA has been developed which probes the early stages of oligomerization of Aβ. Incubation of Aβ solutions at 37°C and pH 7.4 produces soluble oligomers in a concentration- dependent manner. Fresh Aβ42 solutions rapidly form soluble oligomers, whereas Aβ40 solutions require prolonged incubation to produce oligomers. Fresh Aβ42 solutions are more toxic to human neuroblastoma SH-SY5Y cells than Aβ40 solutions, possibly mediated by soluble oligomers. The differences between Aβ42 and Aβ40 could explain the association of the longer form with familial early-onset Alzheimer's disease. We also report a new strategy for solid-phase synthesis of Aβ peptides which gives high yield and purity of the initial crude preparation.
Original language | English |
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Pages (from-to) | 1003-1007 |
Number of pages | 5 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 273 |
Issue number | 3 |
DOIs | |
Publication status | Published - Jul 14 2000 |
Externally published | Yes |
Keywords
- Aggregation
- Alzheimer's disease
- Amyloid
- Oligomerization
- Solid-phase peptide synthesis
- Toxicity
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology