Dresden 2014 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 6: Posters: Membranes and vesicles
BP 6.3: Poster
Montag, 31. März 2014, 17:30–19:30, P3
α-Synuclein insertion into supported lipid bilayer as seen by in situ X-ray reflectivity — •Hendrik Hähl1, Isabelle Möller1, Irena Kiesel2, Dorinel Verdes1, Christian Sternemann2, and Stefan Seeger1 — 1Institute of Physical Chemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich — 2Fakultät Physik/DELTA, TU Dortmund, D-44221 Dortmund
α-Synuclein (αS) is a small 140 residues protein, which is unstructured in its cytosolic form and folds into α-helices upon insertion into the cell membrane. The protein is closely related to the Parkinson disease (PD) via the appearance of aggregates in neuronal cells, which consist mainly of missfolded αS. Yet, neither the normal function of αS nor its role in the pathogenesis of the disease is fully understood. Both seems to be associated with the interaction with the membrane. In its membrane bound form the protein may cause disruption or permeabilization of the membrane. Especially variants appearing in early-onset forms of PD show an increased propensity to membrane destabilization. Here, we applied in situ X-ray reflectivity at high beam energy to monitor the structural changes of supported lipid bilayers upon inclusion of αS and thus aim at a better understanding of the membrane interaction of αS. By comparison with the evolution of a blank bilayer, the wild type form as well as the highly toxic variant E57K were found to intrude deeply into the lipid head groups of the bilayer. Moreover, an observed decrease in the bilayer’s thickness due to the protein insertion shows the protein’s ability to force a remodeling of the membrane.