Researchers find molecule that halts, reverts neurodegeneration caused by Parkinson's disease

The small SynuClean-D molecule interrupts the formation of the alpha-synuclein amyloid fibers responsible for the onset of Parkinson's disease, and reverts the neurodegeneration caused by the disease. The study headed by Universitat Autònoma de Barcelona researchers was published in PNAS.

Parkinson's disease is the second most common incurable neurodegenerative disorder after Alzheimer's disease. It is characterized by the accumulation of protein deposits in dopaminergic neurons (in charge of producing dopamine) in the form of amyloid fibers. These aggregates are formed mainly by the alpha-synuclein protein and in a very complex manner, which makes it complicated to identify molecules which could prevent or revert the process and the neurodegeneration associated with it.

A scientific collaboration led by researchers at the Institute of Biotechnology and Biomedicine (IBB) of the Universitat Autònoma de Barcelona has identified a molecule which halts and reverts this neurodegeneration. After analyzing over 14,000 molecules, they found the SynuClean-D molecule, which inhibits the aggregation of the alpha-synuclein protein and breaks the already formed amyloid fibers, thus preventing the initiation of the process causing the onset of the neurodegenerative Parkinson's disease.

Through experiments conducted with the small Caenorhabditis elegans worm, one of the most commonly used animal models in neurodegenerative diseases, researchers were able to verify that by administering it through food, the molecule was capable of notably reducing alpha-synuclein aggregations, preventing the spread of toxic aggregates and therefore avoiding the degeneration of dopaminergic neurons.

"Everything seems to indicate that the molecule we identified, the SynuClean-D, may provide therapeutic applications for the treatment of neurodegenerative diseases such as Parkinson's in the future", UAB researcher and coordinator of the study Salvador Ventura points out.

To identify SynuClean-D researchers developed a methodology capable of indentifying the alpha-synuclein aggregation inhibitors among thousands of molecules. Once identified, an in vitro biophysical characterization was conducted of their inhibiting activity and tests were run to discover their behavior with human neural cell cultures, before testing it in animal models of the disease (the Caenorhabditis elegans worm). These animals express the alpha-synuclein in the muscle or in dopaminergic neurons. The experiments demonstrated that the administration of the identified inhibitor reduced protein aggregation, improving the mobility of the animal and protecting it from neural degeneration.

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