Press releases
Please quote Nature Chemistry as the source of these items.
The June 2009 issue of Nature Chemistry is now available online.
June 2009
Alzheimer's assemblies identified
Assemblies of twelve units of a protein known as amyloid-β42 are a probable key neurotoxic agent in the development of Alzheimer's disease, according to a study to be published online in Nature Chemistry this week. The identification of such a key toxic species could pave the way for treatments that specifically target the disease in the early stages of development.
Plaques, formed from large assemblies of amyloid-β proteins, are known to be the eventual result of Alzheimer's disease, but recent evidence suggests that small assemblies (or oligomers) of the protein are the toxic agents responsible for the disease symptoms. However, a variety of investigations into how these oligomers arise have, so far, provided conflicting results.
Michael Bowers and co-workers have used a technique called electrospray-ionization ion-mobility mass spectrometry to study the mixture of oligomers formed by amyloid-β42 and some closely related proteins that do not result in disease. The technique allowed the researchers to study both the mass and the geometry of oligomers formed. All the proteins studied formed dimers and tetramers, but only the tetramer from the protein that causes Alzheimer's, amyloid-β42, went on to form a dodecamer (12 units), with the geometry of the tetramer seeming to be the key factor.
In an accompanying News & Views article, David Clemmer and Stephen Valentine say 'One can imagine using the insight gained here to design interventions that are designed to arrest oligomer growth at a specific size.'
Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
Summer L. Bernstein, Nicholas F. Dupuis, Noel D. Lazo, Thomas Wyttenbach, Margaret M. Condron, Gal Bitan, David B. Teplow, Joan-Emma Shea, Brandon T. Ruotolo, Carol V. Robinson & Michael T. Bowers
Published online: 14 June 2009 | doi 10.1038/nchem.247
Bioanalytical chemistry: Protein oligomers frozen in time
David E. Clemmer & Stephen J. Valentine
Published online: 14 June 2009 | doi 10.1038/nchem.264
