Ludwig-Maximilians-Universität, Chair of Metabolic Biochemistry
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Domain formation in phospholipid membranes and the toxicity of alpha-synuclein

TUM München, Faculty of Chemistry; 2008-08-13

Authors/Editors: Tim Bartels
Publication Date: 2008
Type of Publication:
Intracellular deposits of α-Synuclein are hallmark features of Parkinson’s disease on a molecular level. The present dissertation deals with folding and aggregation of the protein in the presence of lipid membranes. It turned out that this lipid-protein interaction depends on membrane curvature and on the presence of intramembrane lipid domains. Therefore, the first part investigates, by means of solid state NMR techniques, the conditions of phase separation and micromechanical properties using appropriate lipid mixtures as a paradigm for neuronal cellular membranes. Selected peptides from the α-Synuclein primary sequence were employed in the second part to characterize regional propensities of the protein for aggregation, folding and membrane binding.

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