Scientists at the University of Toronto Scarborough have mapped out additional chemical secrets behind the advance of Parkinson's disease. Using an electroanalytic technique with a space-age name--voltammetry--they detailed how the alpha-synuclein protein interacting with dopamine in the brain can create protein misfolding and brain cell death.
And the process itself may have some future research cachet, the researchers say. They argue that their technique could be a more cost-effective and speedier way to study protein misfolding. Importantly, they also see researchers as being able to automate the process to screen potential Parkinson's disease treatments. Details are published in the journal Chemical Neuroscience.
Using voltammetry (rather than the more typical microscopy), the team monitored minute changes in electric currents during the interaction of the dopamine and alpha-synuclein proteins. As a result, they were able to determine that higher pH levels and ionic strengths lead to stronger dopamine/alpha-synuclein interactions, which lead to a more rapid buildup of alpha-synuclein protein clusters--a key element of Parkinson's patients.
Such a finding is important here because better understanding Parkinson's and how it operates will ultimately lead to better treatments. The neurodegenerative disease leaves patients with declining cognitive function and increasing loss of motor control. And what is known so far, the researchers remind us, is that as the disease advances, brain cells that produce dopamine die, impairing brain signaling. Subsequently, the alpha-synuclein protein begins to build up in those telltale clusters. And knowing what is behind that buildup could be key to ultimately treating the nasty neurodegenerative disease.
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- check out the journal abstract