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Membrane bound α‐synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain
Author(s) -
Wietek Jonas,
Haralampiev Ivan,
Amoussouvi Aouefa,
Herrmann Andreas,
Stöckl Martin
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.06.034
Subject(s) - biophysics , bilayer , lipid bilayer , membrane , chemistry , amphiphile , sequence (biology) , microbiology and biotechnology , biochemistry , biology , organic chemistry , copolymer , polymer
Cellular pathways involving α‐synuclein (αS) seem to be causative for development of Parkinson's disease. Interactions between αS and lipid membranes appear to be important for the physiological function of the protein and influence the pathological aggregation of αS leading to the formation of amyloid plaques. Upon membrane binding the unstructured αS folds into amphipathic helices. In our work we characterized the penetration depth and probed the local environment of Trp‐residues introduced along the αS 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.