Researchers have combined sophisticated biochemical and imaging techniques to get a glimpse of the stepwise assembly of amyloid fibers in a yeast prion protein. Their findings suggest that these structured fibers form in competition with the amorphous globules that some believe may cause toxicity in amyloid diseases such as Alzheimers and Parkinsons. The researchers say this may have important implications for those designing drugs to prevent formation of the brain-damaging proteins in those diseases.
The researchers reported their findings in the October 2004 issue of the Public Library of Science Biology. They were led by Howard Hughes Medical Institute investigator Jonathan S. Weissman at the University of California, San Francisco. HHMI investigator Ronald D. Vale, also of UCSF, was a co-author of the article.
Working in yeast, Weissman and his colleagues investigated the mechanism by which a prion protein assembles individual polypeptides into long amyloid fibers. These fibers are similar to the amyloid plaques that clog the brains of patients with Alzheimers or Parkinsons disease.
Jennifer Michalowski | EurekAlert!
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