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.

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.

16.11.2006(Innovations Report) -