Premium
The mode of α‐synuclein binding to membranes depends on lipid composition and lipid to protein ratio
Author(s) -
Shvadchak Volodymyr V.,
Yushchenko Dmytro A.,
Pievo Roberta,
Jovin Thomas M.
Publication year - 2011
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.2011.10.006
Subject(s) - membrane , chemistry , biophysics , polarity (international relations) , plasma protein binding , biochemistry , biology , cell
Interactions of the presynaptic protein α‐synuclein with membranes are involved in its physiological action as well as in the pathological misfolding and aggregation related to Parkinsons's disease. We studied the conformation and orientation of α‐synuclein bound to model vesicular membranes using multiparametric response polarity‐sensitive fluorescent probes together with CD and EPR measurements. At low lipid to α‐synuclein ratio the protein binds membranes through its N‐terminal domain. When lipids are in excess, the α‐helical content and the role of the C‐terminus in binding increase. Highly rigid membranes also induce a greater α‐helical content and a lower polarity of the protein microenvironment.