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Environment

Peptide Rounds Up Amyloid-β

Potential Alzheimer's drug renders toxic amyloid-β oligomers into innocuous clumps

by Sophie L. Rovner
August 16, 2010 | A version of this story appeared in Volume 88, Issue 33

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Credit: Heinrich Sticht/ U of Erlangen
D3 (stick structure) gathers toxic amyloid-β oligomers (yellow ribbons) into a nontoxic clump.
Credit: Heinrich Sticht/ U of Erlangen
D3 (stick structure) gathers toxic amyloid-β oligomers (yellow ribbons) into a nontoxic clump.

An experimental Alzheimer’s treatment that targets and traps amyloid-β oligomers improves cognitive performance in mice used as a model for the disease, according to a study (ACS Chem. Neurosci., DOI: 10.1021/cn100057j). Dieter Willbold of Heinrich Heine University Düsseldorf and the Jülich Research Center, in Germany, and colleagues believe the findings support the increasingly popular theory that soluble amyloid-β oligomers, rather than insoluble fibrils and plaques, are the neurotoxic species that cause the brain disease. The researchers showed that the treatment, a peptide known as D3, binds to amyloid-β oligomers, altering their conformation and inducing them to coalesce into huge, nontoxic clumps. D3 is much less capable of binding amyloid-β monomers, Willbold says, so the treatment won’t interfere with the monomers’ normal functions, which are still unclear. Cell culture and animal assays to date have shown no toxicity for the compound, he adds. The researchers have patented the peptide in Europe and are negotiating with pharmaceutical companies interested in developing it further.

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