-Short Biography (Education, Internships, maybe Hobbies….)

In 2005 Dr. Martin Stöckl graduated from the University of Bayreuth holding a diploma in biochemistry. In his thesis he focused on the characterization of protein folding processes. He continued his academic training as a PhD-student in the workgroup of Prof. Andreas Herrmann at the Humboldt University in Berlin, where he graduated in 2008 with a doctor’s degree in biophysics. His thesis entitled “”Giant vesicles – an ideal tool to study lateral phospholipid distribution and domain dependent protein membrane interactions” included work on the identification of factors which have an impact on the interactions between α-synuclein and phospholipid membranes and the characterization of the membrane organization using fluorescence lifetime imaging. He stayed in the group for an additional year as a postdoctoral researcher to chracterize the impact of statins on cholesterol flux in hepatocytes. In 2010 he joined the Nanobiophysics group with a DAAD-fellowship, where he is now studying the mechanisms by which oligomeric α-synuclein species impair membrane integrity using a combination of AFM and fluorescence techniques

-Contact Information -

Dr. MartinStöckl


University of Twente

Institute for Nanotechnology MESA+

Zuidhorst ZH152

Drienerlolaan 5

7522 NB  Enschede, the Netherlands

PO-box 217

7500AE Enschede, the Netherlands

P +31-(0)53-489-3161

F +31-(0)53-489-2150

-Own Research in NBP-

TOPIC: Identifying the mechanisms underlying the impairment of membrane integrity caused by α-synuclein oligomers

Parkinson’s Disease (PD) is one of the most prevalent neurodegenerative diseases. The progression of the disease is accompanied by a loss of dopaminergic neurons. Although the exact cause of neuronal death is not known, the protein α-synuclein and its interaction with cellular membranes seem to play a major role during the development of PD. In order to identify the underlying mechanisms by which oligomeric α-synuclein species cause an impairment of the membrane integrity, I study these processes using vesicular and planar membrane model systems.

Using large unilamellar vesicles (LUV) labeled with fluorescent lipids I’m characterizing the impact of different oligomeric α-synuclein species on membrane permeability and lipid flip-fliop. While these approaches are ideally suited to describe the effects of α-synuclein oligomers on these processes, they can’t visualize the events at the α-synuclein binding sites. Therefore, I will use recently described suspended asymmetric phospholipid bilayers which are able to closely mimic the situation at the plasma membrane of cells to study α-synuclein membrane interactions. In this model system, atomic force microscopy will allow the identification of the binding sites, the measurement of penetration depths of the oligomers into the phospholipid bilayers, and will detect a possible membrane thinning and membrane defects, while fluorescence lifetime imaging microscopy using membrane probes sensitive to the lipid organization will allow to assess the membrane order.

The results of the project hopefully will give valuable insights in the mechanisms underlying the pathophysiology of PD and therefore may yield valuable points of leverage for the development of a cure to the disease.

Publications of interest

(Means publications that either describe your work or your own)


M. Stöckl, P. Fischer, E. Wanker, & A. Herrmann, Alpha-synuclein selectively binds to anionic phospholipids embedded in liquid-disordered domains, J. Mol. Biol., 375(5) (2008), 1394-1404


M. Stöckl, A.P. Plazzo, T. Korte, & A. Herrmann, Detection of Lipid Domains in Model and Cell Membranes by Fluorescence Lifetime Imaging Microscopy of Fluorescent Lipid Analogues, J. Biol. Chem., 283(45) (2008), 30828-30837


M.T. Stöckl & A. Herrmann, Detection of lipid domains in model and cell membranes by fluorescence lifetime imaging microscopy, BBA – Biomem, 1798(7), (2010), 1444-1456