Project:  Interactions of the Parkinson’s disease related protein α-synuclein with model membranes

Martin Stöckl

Parkinson’s disease (PD) is a neurodegenerative disease accompanied with the loss of neurons. Studies indicate that α-synuclein plays a causative role during the development of PD. For example three disease related missense mutations have been discovered in the α-synuclein gene. In addition amyloid fibrils formed from α-synuclein can be found in protein deposits typical for the PD. Previous studies showed that structural properties of α-synuclein and its propensity to form amyloid fibrils are altered by membrane interactions. The association of fluorescence-labeled α-synuclein variants with different types of giant unilamellar vesicles (GUVs) is investigated using confocal microscopy finding that α-synuclein binds with high affinity to anionic phospholipids, when they are embedded in a liquid-disordered as opposed to a liquid-ordered environment.

Publications:

Stöckl, M., Fischer, P., Wanker, E., Herrmann, A. (2008)
α-Synuclein Selectively Binds to Anionic Phospholipids Embedded in Liquid-Disordered domains,
J. Mol. Biol. 375, 1394-1404.

Suopanki, J., Götz, C., Lutsch, G., Schiller, J., Herrmann, A., Wanker, E.E. (2006)
Interaction of huntingtin fragments with brain membranes - clues to early dysfunction in Huntington's disease.
J. Neurochem. 96, 870-84.