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January 1st, 2008
Alzheimer's intermediate characterised by SS NMR
A team of chemists at the University of Illinois Chicago has characterized the molecular structure of a molecular intermediate in the development of Alzheimer's disease. Using NMR the team has identified a precursor to the misfolded proteins known as plaque-forming amyloid, which is involved in Alzheimer's disease. The same results may also provide clues to understanding and treating Parkinson's and Creutzfeldt-Jakob disease which also involve protein misfolding.
Effective treatment for Alzheimer's remains elusive despite the best efforts of biomedical researchers and drug discovery teams the world over. One of the problems facing drug developers is how to explain the role of amyloid plaques. Whether or not they are a cause or a symptom of the disease is not yet known for sure, although they are certainly a hallmark of this debilitating and lethal disease. Amyloid fibrils are clumps of a fibre-like protein material that is misfolded and is present at nerve cells damaged in this devastating and tragic neurodegenerative diseases.
Now, Yoshitaka Ishii and his colleagues, Sandra Chimon, Medhat Shaibat, Christopher Jones, Diana Calero, and Buzulagu Aizezi, have trapped and characterized a crucial intermediate in the formation of amyloid plaque fibres, or fibrils, showing tiny spheres averaging just twenty nanometres in diameter assembling into sheet-like structures comparable to that seen in the formation of fibrils.
University of Illinois Chicago
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