E-Mail
IMAGE: Scientists from the University of Konstanz and the Free University of Amsterdam, in collaboration with the Bruker BioSpin development team, have succeeded for the first time in the direct spectroscopic...
view more
Credit: Malte Drescher Lab - University of Konstanz
The protein α-synuclein is one of the most abundant proteins in the human brain. It is often referred to as the "Parkinson protein", as deposition of this protein in brain cells is a hallmark of Parkinson's disease. Despite the high interest of biomedical research in the protein, many questions concerning the function and physiology of α-synuclein in living cells still remain to be answered. For example, it was previously unclear whether and to what extent the protein binds to and interacts with internal cell components such as membranes. As such processes could play a role in the development of the disease, the team led by Konstanz-based physical chemist Professor Malte Drescher used the further development of an established measurement method called "electron paramagnetic resonance spectroscopy" (EPR spectroscopy) to learn more about the binding properties of the "Parkinson protein". The study, published in the scientific periodical "The Journal of Physical Chemistry Letters", furnishes proof of concept that the advanced method is fundamentally suitable for elucidating protein-lipid interactions in cells. Furthermore, this first practical test yielded direct evidence of the binding of α-synuclein to intracellular membranes.