Free Newsletter
Register for our Free Newsletters
Newsletter
Zones
Advanced Composites
LeftNav
Aerospace
LeftNav
Amorphous Metal Structures
LeftNav
Analysis and Simulation
LeftNav
Asbestos and Substitutes
LeftNav
Associations, Research Organisations and Universities
LeftNav
Automation Equipment
LeftNav
Automotive
LeftNav
Biomaterials
LeftNav
Building Materials
LeftNav
Bulk Handling and Storage
LeftNav
CFCs and Substitutes
LeftNav
Company
LeftNav
Components
LeftNav
Consultancy
LeftNav
View All
Other Carouselweb publications
Carousel Web
Defense File
New Materials
Pro Health Zone
Pro Manufacturing Zone
Pro Security Zone
Web Lec
Pro Engineering Zone
 
 
 
News

New finding may provide insight on Alzheimer's and Huntington's disease

National Science Foundation : 08 June, 2005  (New Product)
After years of intense work, researchers have discovered the 3-dimensional structure of a miniscule, yet mighty, region of a protein that forms deleterious rope-like structures in the brain. Known as amyloid fibrils, the proteins are associated with the degenerative brain disorders Alzheimer's, Parkinson's and Huntington's diseases, and so-called prion diseases like mad cow. This particular region of the protein catalyzes the formation of a 'molecular zipper,' which pulls proteins together to form the stubbornly stable clumps.
After years of intense work, researchers have discovered the 3-dimensional structure of a miniscule, yet mighty, region of a protein that forms deleterious rope-like structures in the brain. Known as amyloid fibrils, the proteins are associated with the degenerative brain disorders Alzheimer's, Parkinson's and Huntington's diseases, and so-called prion diseases like mad cow. This particular region of the protein catalyzes the formation of a 'molecular zipper,' which pulls proteins together to form the stubbornly stable clumps.

Knowing the structure will help researchers devise new treatments for the more than two-dozen human diseases associated with fibrils, which are attributed to killing neurons and other types of cells. Effective therapeutics may reverse the zipping to break down persistent fibrils or prevent them from forming in the first place.

The work appears in the June 9 issue of the journal Nature.

By studying a specific yeast protein that aggregates similarly to the fibrillar proteins associated with animal diseases, David Eisenberg, his team at the University of California, Los Angeles, and international colleagues determined that a region of these fibril-forming proteins forms two sheets that 'zip together.' This coupling, occurring along a self-guided track, squeezes out water molecules to form a dry, persistent structure that helps account for the tenacity of fibril build ups.

This abnormally dry, zipped-up protein is completely insoluble, that is, it does not dissolve in water, which is a hallmark of amyloid fibrils. In people with Alzheimer's disease, for example, the build up of fibrils in the brain is commonly referred to as plaque.

After years of solo work on the protein's structure, Eisenberg teamed with Christian Reikel, an expert who studies the crystal structures of small-scale molecules at the European Synchrotron Radiation Facility. Using a technology that allowed them to 'see' the protein's 3-dimensional structure, the combined group is the first to document the molecular structure of a fibril, a feat that has eluded researchers for decades.
Bookmark and Share
 
Home I Editor's Blog I News by Zone I News by Date I News by Category I Special Reports I Directory I Events I Advertise I Submit Your News I About Us I Guides
 
   © 2012 NewMaterials.com
Netgains Logo