Mireille Claessens

Mireille Claessens obtained her PhD training in the laboratories of Physical Chemistry and Colloid Sciences (with F. Leermakers and M.A. Cohen Stuart) and Plant Physiology (with F.A. Hoekstra) at Wageningen University, the Netherlands. After receiving her PhD degree in 2003 she moved to the group of A. Bausch at the Technical University of Munich where she investigated the physical properties of cytoskeletal networks. In 2008 she joined the Nanobiophysics group at the University of Twente as an associate professor. In 2009 she was awarded a VIDI grant that allows her to study supra-fibrillar amyloid aggregates and their implications for cellular functioning. In September 2013, she became chair of the NBP-group.

-Contact Information -

Prof. Dr. Ir. Mireille Claessens

Nanobiophysics

University of Twente

Institute for Nanotechnology MESA+

Zuidhorst ZH163

Drienerlolaan 5

7522 NB  Enschede, the Netherlands

PO-box 217

7500AE Enschede, the Netherlands

P +31-(0)53-489-3157

F +31-(0)53-489-1105


m.m.a.e.claessens@utwente.nl

-Own Research in NBP-

TOPIC: Functional and disease related interactions of natively unfolded proteins

In my work I aim at understanding the physical principles underlying the organization, dynamics and mechanical properties of proteins and protein filaments. Currently my work focuses on the function of the natively unfolded protein alpha-synuclein and its role in neurodegenerative diseases. In Parkinson’s disease alpha-synuclein aggregates into fibrils and forms supra-fibrillar plaques that are the pathological hallmark of the disease. Why and how the fibrillization of alpha-synuclein is toxic for cells is not understood. We try to get physicochemical insight into alpha-synuclein aggregation and toxicity using reconstituted protein and cellular model systems.

Current projects

1.

Supra-fibrillar amyloid aggregates

a.

Material properties of subra- fibrillar aggregates

b.

Supra-fibrillar α- Synuclein aggregates

2.

The amyloid pore hypothesis

3.

Amyloid aggregation in confinement

4.

Interactions between alpha-synuclein and the cytoskeleton

5.

Alpha-synuclein in neuronal cells

6.

Functional amyloid scaffolds

Publications of interest

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

1.

H. Chaudhary, V. Subramaniam, M.M.A.E. Claessens. 2014. α-Synuclein fibrillation plays an essential role in membrane disruption. FEBS Letters DOI: 10.1016/j.febslet.2014.10.016

2.

Semerdzhiev S., D.R. Dekker, V. Subramaniam, M.M.A.E. Claessens. 2014. Self-assembly of protein fibrils into supra-fibrillar aggregates: bridging the nano- and mesoscale. ACS Nano 8: 5543-5551

3.

Stefanovic A.N.D., M.T. Stöckl, M.M.A.E. Claessens, V. Subramaniam 2014. α -synuclein oligomers distinctively permeabilize complex model membranes. FEBS Journal 281: 2823- 2350

4.

Zijlstra N., C. Blum, I.J.M. Segers-Nolten, M.M.A.E. Claessens, V. Subramaniam. 2012. Molecular composition of sub-stoichiometrically labeled α-synuclein oligomers determined by single- molecule Photobleaching. Angewandte Chemie International Edition 51: 8821–8824

5.

van Rooijen, B. D., M. M. A. E. Claessens, and V. Subramaniam. 2010. Membrane permeabilization by oligomeric alpha-synuclein: in search of the mechanism. Plos One 5: e14292.

6.

Lieleg, O., M. M. A. E. Claessens, and A. R. Bausch. 2010. Structure and Dynamics of Crosslinked Actin Networks. Soft Matter 6: 218-225

7.

van Rooijen, B. D., K. A. van Leijenhorst-Groener, M. M. A. E. Claessens, and V. Subramaniam. 2009. Tryptophan Fluorescence Reveals Structural Features of α-Synuclein Oligomers. Journal of Molecular Biology 394:826-833

8.

Claessens, M. M. A. E., C. Semmrich, L. Ramos, and A. R. Bausch. 2008. Helical twist controls the thickness of F-actin bundles. Proceedings of the National Academy of Sciences of the United States of America 105:8819-8822.

9.

Lieleg, O., M. M. A. E. Claessens, C. Heussinger, E. Frey, and A. R. Bausch. 2007. Mechanics of bundled semiflexible polymer networks. Physical Review Letters 99: 088102.

10.

Claessens, M. M. A. E., M. Bathe, E. Frey, and A. R. Bausch. 2006. Actin-binding proteins sensitively mediate F-actin bundle stiffness. Nature Materials 5:748-753.

11.

Claessens, M. M. A. E., R. Tharmann, K. Kroy, and A. R. Bausch. 2006. Microstructure and viscoelasticity of confined semiflexible polymer networks. Nature Physics 2:186-189.