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Amyloid plaques are thought to cause the devastating neurodegenerative Alzheimer’s disease.

Until recently the fibrils made of small proteins of amyloid-beta where thought to be the toxic element that kills nerve cells. Recently Yoshitaka Ishii, associate professor of chemistry, University of Illinois at Chicago, was able to capture and characterize a crucial intermediate step in the formation of amyloid plaque fibers, or fibrils, that are more than 10 times as poisonous as the amyloid-beta fibrils.

Ishii and co-workers are the first to confirm that the intermediate stage of amyloid is more toxic than the final form of the fibrils. The researchers are confident that that they will be able to make a complete determination of the intermediate structure and once completed their findings may provide pharmaceutical manufacturers with the information they need to create drugs that will prevent interaction between the toxic molecules and nerve cells.

Researchers feel their method can also be applied to structural studies of proteins associated with other neurodegenerative diseases, including Parkinson’s, and prion diseases, such as Creutzfeldt-Jacob (Mad Cow).

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