In vitro aging of ß-amyloid protein causes peptide aggregation and neurotoxicity
Abstract ß-Amyloid peptide forms the senile plaques of Alzheimer's disease and has been
previously demonstrated to have both trophic and toxic effects on neurons in vitro. We report
here that synthetic ß-amyloid peptide shows both aggregation and neurotoxicity after a 2–4
day incubation period, but is neurite-promoting and not toxic in its initially solubilized state.
SDS-PAGE characterization shows that newly solubilized ß-amyloid is predominantly
monomeric whereas incubated peptide has several high molecular weight species.
previously demonstrated to have both trophic and toxic effects on neurons in vitro. We report
here that synthetic ß-amyloid peptide shows both aggregation and neurotoxicity after a 2–4
day incubation period, but is neurite-promoting and not toxic in its initially solubilized state.
SDS-PAGE characterization shows that newly solubilized ß-amyloid is predominantly
monomeric whereas incubated peptide has several high molecular weight species.
Abstract
ß-Amyloid peptide forms the senile plaques of Alzheimer's disease and has been previously demonstrated to have both trophic and toxic effects on neurons in vitro. We report here that synthetic ß-amyloid peptide shows both aggregation and neurotoxicity after a 2–4 day incubation period, but is neurite-promoting and not toxic in its initially solubilized state. SDS-PAGE characterization shows that newly solubilized ß-amyloid is predominantly monomeric whereas incubated peptide has several high molecular weight species.
Elsevier
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