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ORNL, UTGSM study compares structures of Huntington's disease protein
Date:7/16/2014

ptides, whereas the normal version makes bigger aggregates, gathering seven or eight peptides together.

These data on the very early stages of protein aggregate formation support a growing focus of the research in the amyloid field. Amyloid disorders, such as Parkinson's, Alzheimer's and Huntington's, all involve protein aggregation phenomena leading to a disease.

"There is no strong correlation between neuronal cell loss and the amount of protein aggregates found in the brain," Stanley said. "You could have a case with a lot of aggregates but minimal symptoms -- and you can find the converse. Researchers think there must be something happening at the earliest stage that's giving rise to toxicity."

Stanley says the team hopes to continue its research to obtain higher-resolution structural data and refine their understanding of the huntingtin protein.

"We'd like to use this small-angle neutron scattering technique in combination with others to get a better idea for how these early structures are forming and also ask the question -- are they toxic or not?" Stanley said.


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Contact: Morgan McCorkle
mccorkleml@ornl.gov
86-557-407-308
DOE/Oak Ridge National Laboratory
Source:Eurekalert  

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ORNL, UTGSM study compares structures of Huntington's disease protein
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