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Parkinson’s: Bend in Molecule Trans­forms Protein into Aggregation Inhibitor

Structurally altered α-synuclein no longer forms toxic aggregates and prevents other proteins forming clumps

Jülich/Düsseldorf, 28 July 2015 – Aggregates of the body’s own protein α-synuclein in the brain are believed to be a cause of Parkinson’s disease. Researchers at Jülich and Düsseldorf have observed how the protein loses its fatal tendency to aggregate when its molecular structure is altered at a critical site. The modified α-synuclein also inhibits the aggregation of proteins involved in Alzheimer’s disease and type 2 diabetes. The effect, which the researchers have published in the current issue of the journal Angewandte Chemie, could provide a basis for new therapeutic approaches and help to explain the striking similiarities between various neurodegenerative diseases.

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