FINDINGS:
Alzheimer's disease is the leading cause of late-life dementia. An increasing body of evidence has linked assemblies of a common peptide, the amyloid-? protein, to the disease. While plaques formed from large assemblies of this protein are known to be the eventual result of Alzheimer's, recent evidence suggests that small assemblies — or oligomers — of amyloid-? are the toxic agents responsible for the disease symptoms.
In this research, scientists used mass spectrometry to study the mixture of oligomers formed by the amyloid-?42 protein. While many types of amyloid-? assemblies have been described, the researchers found that oligomers made up of 12 units of amyloid-?42 appear to be a key neurotoxic agent in the development of Alzheimer's.
IMPACT:
Discovering the pathways of assembly may be critical in determining therapeutic targets for Alzheimer's. The identification of such a key, specific toxic assembly could pave the way for treatments that target the disease in the early stages of development.
AUTHOR:
UCLA neurology professor David Teplow, a member of the research team, is available for interviews.
JOURNAL:
The research appears online this week in the journal Nature Chemistry.
BACKGROUND:
The researchers used a technique known as electrospray-ionization ion-mobility mass spectrometry to study the mixture of oligomers formed by amyloid-?42 and some closely related proteins that do not result in disease. The technique allowed the team to observe both the mass and geometry of the oligomers formed.
FUNDING:
Funding from the National Institutes of Health, the National Science Foundation, the Alfred P. Sloan Foundation, the David and Lucile Packard Foundation, and the Biotechnology and Biological Sciences Research Council supported this work.
MEDIA CONTACT:
Mark Wheeler | 310-794-2265 | [email protected]
