Researchers have begun to explore the protein that is involved in Huntington's disease in a bid to learn more about how it works.
A study undertaken at the Department of Energy's Oak Ridge National Laboratory (ORNL) has shown there are notable differences in the structure of normal and pathological proteins that are part of the condition.
The aim of the research was to acquire a foundational understanding of the structure of huntingtin, which is a clump of protein fragments that is brought about by a genetic mutation. This eventually leads to the disease.
With a basic knowledge of huntingtin and how it functions, there is the potential for scientists to ascertain the structure of the neurodegenerative disorder itself - which could pave the way for treatments or cures.
Chris Stanley from ORNL said: "We compared the normal and disease versions of the protein to see how they change over time. You can see there's a discrepancy all the way from the early stages to the end-state fibrils."
It transpired there were substantial discrepancies in the shapes of the normal and damaged proteins. The latter come together to make clumps of one or two peptides, while the healthy version makes larger ones - more like seven or eight.
The findings - which were published in Biophysical Journal - follow a similar path to a great deal of research that is taking place at the moment in the amyloid field. Disorders of this kind - such as Parkinson's and Alzheimer's - involve the accumulation of proteins. For instance, the aggregation of amyloid-beta is generally regarded as a hallmark of Alzheimer's.
Valerie Berthelier of the University of Tennessee Graduate School of Medicine, who was co-leader of the study alongside Mr Stanley, commented that this was just the "very first" step. If the researchers could ascertain if any of the structures are toxic, this could lead to being able to design treatments, she said.
Huntington's is a hereditary disorder of the central nervous system and has a wide range of symptoms.
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