Journal
FEBS LETTERS
Volume 587, Issue 16, Pages 2572-2577Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2013.06.034
Keywords
alpha-synuclein; Lipid bilayer; Fluorescence spectroscopy; Penetration depth
Funding
- Max-Delbruk-Center for Molecular Medicine
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Cellular pathways involving alpha-synuclein (alpha S) seem to be causative for development of Parkinson's disease. Interactions between alpha S and lipid membranes appear to be important for the physiological function of the protein and influence the pathological aggregation of alpha S leading to the formation of amyloid plaques. Upon membrane binding the unstructured alpha S folds into amphipathic helices. In our work we characterized the penetration depth and probed the local environment of Trp-residues introduced along the alpha S sequence. We could show that while the entire helix is well embedded in the lipid bilayer, segments with a shallower penetration and supposable higher flexibility exist. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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