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Release date:
12-5-01
Contact: Deb Hammacher, Associate Director, 404-727-0644, or dhammac@emory.edu

Molecular self-assembly research uncovers new understanding of Alzheimer's disease

In their quest to understand the structural and energetic basis of molecular self-assembly, the laboratory of David Lynn, Emory's Candler Professor of Chemistry and Biology, has helped solve the first structure of an amyloid fibril, shedding new light on Alzheimer's and other diseases. A collaboration with researchers at Argonne National Laboratory and the University of Chicago has established the beautifully symmetrical array of peptides in the fibril. This structure spontaneously self-assembles, a process like many others in biology, including protein folding, vessicle formation and even the organogenesis of multicellular organisms, but in this case to form abnormal fibril arrays toxic to human neurons. The structure now, for the first time, offers the possibility to define the pathway to assembly, the structural and energetic contributions to fibril stability, and the rational design of compounds to regulate fibril formation and the onset of Alzheimer's disease. Such knowledge fundamentally expands our understanding of the dozens of known amyloid diseases.

The abnormal fibril arrays the group studies, which can grow several millimeters long, are prevalent in the amyloid plaques associated with Alzheimer's disease. These plaques decrease brain matter, which can in turn disrupt neural function, "like going into a computer and ripping out wires. The same connections are not there," Lynn says. While there is a distinct correlation between the presence of the fibrils and Alzheimer's disease, what causes the toxicity that disrupts neural activity remains to be discovered.

Click here to read a recent article on the project

 

 


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