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. 2003 Apr 18;300(5618):486-9.
doi: 10.1126/science.1079469.

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Rakez Kayed  1 , Elizabeth Head, Jennifer L Thompson, Theresa M McIntire, Saskia C Milton, Carl W Cotman, Charles G Glabe
Affiliations

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Rakez Kayed et al. Science. .

Abstract

Soluble oligomers are common to most amyloids and may represent the primary toxic species of amyloids, like the Abeta peptide in Alzheimer's disease (AD). Here we show that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomers regardless of sequence. The in vitro toxicity of soluble oligomers is inhibited by oligomer-specific antibody. Soluble oligomers have a unique distribution in human AD brain that is distinct from fibrillar amyloid. These results indicate that different types of soluble amyloid oligomers have a common structure and suggest they share a common mechanism of toxicity.

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Comment in

  • Good and bad amyloid antibodies.
    Mattson MP, Chan SL. Mattson MP, et al. Science. 2003 Sep 26;301(5641):1847-9. doi: 10.1126/science.301.5641.1847. Science. 2003. PMID: 14512605 No abstract available.

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