Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Rakez Kayed, Elizabeth Head, Jennifer L. Thompson, Theresa M. McIntire, Saskia C. Milton, Carl W. Cotman, Charles G. Glabel

Research output: Contribution to journalArticle

3132 Scopus citations

Abstract

Soluble oligomers are common to most amyloids and may represent the primary toxic species of amyloids, like the Aβ 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.

Original languageEnglish (US)
Pages (from-to)486-489
Number of pages4
JournalScience
Volume300
Issue number5618
DOIs
StatePublished - Apr 18 2003

ASJC Scopus subject areas

  • General

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    Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabel, C. G. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science, 300(5618), 486-489. https://doi.org/10.1126/science.1079469