Alzheimers disease, Parkinsons disease, type II diabetes, the human version of mad cow disease and other degenerative diseases are more closely related at the molecular level than many scientists realized, an international team of chemists and molecular biologists reported April 29 in the online version of the journal Nature (print version to follow).
Harmful rope-like structures known as amyloid fibrils, which are linked protein molecules that form in the brains of patients with these diseases, contain a stack of water-tight "molecular zippers," the scientists report.
"We have shown that the fibrils have a common atomic-level structure," said David Eisenberg, director of the UCLADepartment of Energy Institute of Genomics and Proteomics, a Howard Hughes Medical Institute investigator and a member of the research team. "All of these diseases are similar at the molecular level; all of them have a dry steric zipper. With each disease, a different protein transforms into amyloid fibrils, but the proteins are very similar at the atomic level."
The research, while still preliminary, could help scientists develop tools for diagnosing these diseases and, potentially, for treating them through "structure-based drug design," said Eisenberg, a UCLA professor of chemistry and molecular biology.
The researchers, including scientists with the European Synchrotron Radiation Facility in Grenoble, France, report 11 new three-dimensional atomic protein structures, including those for both of the main proteins that form amyloid fibrils in Alzheimers disease.
"It has been a joy to see so many new structures," said Michael Sawaya, a research scientist with UCLA and the Howard Hughes Medical Institute and a member of the team. "Each one is like a Christmas present. Now that we have so many of these that we can classify, I am thrilled to see each three-dimensional arrangement of atoms, what the structural similarities and differences ar
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Contact: Stuart Wolpert
swolpert@support.ucla.edu
310-206-0511
University of California - Los Angeles
30-Apr-2007