Christian studied at the universities in Freiburg & Rostock, Germany. There, he obtained a degree in sports medicine & biology. During his master thesis, he successfully optimized and combined molecular-biology based approaches for detection of lowest quantities of allergen in food (published as book *). Feeling the need to think outside of the box, he took a sabbatical leave and crossed the North American continent twice by bicycle to raise awareness for global warming. Following his return, he joined the group of Tissue regeneration at the University of Twente where he studied the effect of the protein sonic hedgehog on angiogenesis (PNAS 2012). Due to his high interests in cell culture and microscopy techniques, he started as a PhD in the group of Nanobiophysics in which he is exploring the influence of supra fibrillar amyloid assemblies on the cytoskeleton.

C. C. Raiss(MSc)


University of Twente

Institute for Nanotechnology MESA+

Zuidhorst ZH166

Drienerlolaan 5

7522 NB  Enschede, the Netherlands

PO-box 217

7500AE Enschede, the Netherlands

P +31-(0)53-489-3466

Project: Supra Fibrillar Amyloid Assemblies on the cytoskeleton

Parkinson`s disease (PD) belongs to the group of neurodegenerative diseases. Hallmark of PD is the degeneration & loss of neurons in the in the brain (substantia nigra) which causes multiple symptoms such as impairment of motoric and cognitive functions. Until today, no cure was found.

Along with the dying neurons during the progression of PD, the formation of protein clumps and fibrils inside these cells are observed. These clumps or fibrils are named Lewy Bodies (LB) and Lewy Neurites (LN) and mainly consist of a protein called α- synuclein. In PD, this protein aggregates to from undissolvable clumps and transform into LB or LN. The actual effect of these inclusions on tissue & neurons, how and why they develop is not clear.

The cytoskeleton is the cellular "skeleton" contained within the cytoplasm. It consists of various monomeric proteins that polymerize into fibrils and filaments to fulfil their biological function. It is described (Sousa et al., 2009) that the α- Synuclein interacts with actin, one of the cytoskeletal proteins, yet the role and strength of the interaction is not fully determined. Taking into account that the cytoskeleton plays an important role not only in cellular transport mechanisms, but also in cellular movement and stability, cell functions might be significantly affected by formation and presence of α- synuclein fibrils.

In this project, we observe on the one hand the formation, structure and effect of LB or LN on neurons. On the other hand, we study the interaction of α-synuclein and cytoskeletal proteins on molecular level.

Colocalisation of α- Synuclein with the cytoskeleton.: SH-SY5Y cells expressing GFP-tagged α-Α-synuclein (green) with labeld cytoskeleton (red) & α- α-synuclein (cyan).

Publications of interest


Α- Synuclein and Its A30P Mutant Affect Actin Cytoskeletal Structure and Dynamics- Vítor L. Sousa*,,,, Serena Bellani,, Maila Giannandrea, Malikmohamed Yousuf, Flavia Valtorta*, Jacopo Meldolesi* and Evelina Chieregatti


Exogenous -synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells - Kelvin C. Luk, Cheng Song, Patrick O’Brien, Anna Stieber, Jonathan R. Branch, Kurt R. Brunden, John Q. Trojanowski, and Virginia M.-Y. Lee

* ISBN-10:3639091795