After Alzheimer’s, Parkinson’s is the most common neurodegenerative disease in the world. More than six million people worldwide suffer from it. In this disease, alpha-synuclein proteins form thread-like structures called fibrils. When these fibrils clump together, they probably damage nerve cells. A research team has now shown for the first time how lipids bind to the fibril surface and influence the arrangement of the synuclein proteins within the fibrils. As it demonstrated, the drug candidate anle138b binds into a tube-shaped hole inside such a lipidic fibril. The researchers’ findings could open new approaches to diagnosing and treating Parkinson’s disease.
“Our findings underline that we need to study alpha-synuclein fibrils also in the presence of lipids if we want to understand the molecular basis of alpha-synuclein related pathologies,” Director of the Max PIanck Institute (MPI) for Multidisciplinary Sciences and MBExC member Christian Griesinger comments.
