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Parkinson's disease is the second most common neurodegenerative disease. Over the last 30 years, studies have shown that a protein called alpha-synuclein abnormally aggregates in people with Parkinson's disease, becoming toxic to neurons in a region of the brain that controls movement. This leads to tremor, rigidity and slowness of movement.

Now, in a study published in the Proceedings of the National Academy of Sciences, Yale School of Medicine researchers report they have been able to prevent the buildup of alpha-synuclein in a mouse model of Parkinson's, more than doubling how long the animals live.

More research is needed, but the findings could inform the development of new therapies that block the toxicity of alpha-synuclein.

Arthur Horwich, M.D., Sterling professor emeritus of genetics at Yale School of Medicine and senior author of the new study, has spent decades studying protein misfolding and its prevention by so-called molecular chaperones. These specialized proteins have been shown by his group and others to specifically bind not-yet-folded and misfolded proteins, preventing them from sticking to each other and forming harmful aggregates, and then releasing them to find their correct form.

While Horwich's team was conducting this research, scientists were discovering that neurodegenerative diseases, such as Alzheimer's and Parkinson's diseases, were associated with characteristic misfolded proteins that molecular chaperones apparently could not effectively thwart. This led Horwich and his team to wonder whether other molecules could potentially provide such protection.

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