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Protein 'wires' common in Parkinson's disease now shown in the lab

The misfolding of proteins in brain cells, commonly seen in Parkinson’s Disease, can be imitated in a laboratory setting very well, on a nanoscale. The fibrils, tiny ‘wires’, formed by proteins present in healthy brain cells, are thus shown to be different from the mutant proteins, only seen in patients suffering from an hereditary form of Parkinson.

Scientists Martijn van Raaij, Ine Segers-Nolten and Vinod Subramaniam of the University of Twente show these clear differences in their publication in Biophysical Journal of this week. Comparable fibrils could play a role in other neurodegenerative diseases like Alzheimer and Creutzfeld Jakob.

The actual cause of Parkinson’s disease is, almost two hundred years after the First publication of the Britisch doctor after whom the disease is named, still unknown. Apart from clinical research among patients, research on a cellular and molecular level is performed. It has already been established that clustering or misfolding of proteins in brain cells plays a crucial role.

Martijn van Raaij, who is a PhD-student within the Biophysical Engineering group of prof Vinod Subramaniam, has looked at this clustering process using an Atomic Force Microscope: a microscope that scans a surface with a tiny needle and is able to visualize individual protein fibrils.

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The a-synuclein protein forms fibrils with typical lengths of micrometers. This process of forming of wires is important in the search for causes of Parkinson’s disease and other diseases. Van Raaij’s new results point in that direction as well: he shows morphological differences between fibrils of the proteins almost everyone has in his or her brain cells, and mutant proteins only very rarely shown in families suffering from a hereditary form of Parkinson. These differences in shape are, for example, seen in the diameters and the distance between the peaks the microscope ‘feels’ moving over the surface.

Wiebe van der Veen | alfa
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