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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Aged
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Aged, 80 and over
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Alzheimer Disease / metabolism
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Alzheimer Disease / pathology
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Amyloid / chemistry
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Amyloid / toxicity
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Amyloid beta-Peptides / analysis
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Amyloid beta-Peptides / chemistry*
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Amyloid beta-Peptides / immunology
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Amyloid beta-Peptides / toxicity
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Animals
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Antibodies / immunology
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Antibody Specificity
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Biopolymers / analysis
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Biopolymers / chemistry
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Biopolymers / toxicity
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Brain / pathology
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Brain Chemistry
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Cell Survival
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Humans
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Microscopy, Confocal
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Microscopy, Electron
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Molecular Mimicry
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Neurofibrillary Tangles / chemistry
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Peptide Fragments / chemistry
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Peptide Fragments / immunology
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Protein Conformation
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Rabbits
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Solubility
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Tumor Cells, Cultured
Substances
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Amyloid
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Amyloid beta-Peptides
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Antibodies
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Biopolymers
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Peptide Fragments
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amyloid beta-protein (1-42)