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Therefore, the interaction of \u03b1S with membranes composed of zwitterionic (POPC) and anionic (POPG) lipids was investigated through the mobility of spin labels attached to the protein. Differently labelled variants of <jats:italic>\u03b1<\/jats:italic>S were produced, containing a spin label at positions 9, 18 (both helix 1), 69, 90 (both helix 2), and 140 (C terminus). Protein binding to POPC\/POPG vesicles for all but \u03b1S140 resulted in two mobility components with correlation times of 0.5 and 3 ns, for POPG mole fractions &gt;0.4. Monitoring these components as a function of the POPG mole fraction revealed that at low negative\u2010charge densities helix 1 is more tightly bound than helix 2; this indicates a partially bound form of \u03b1S. Thus, the interaction of <jats:italic>\u03b1<\/jats:italic>S with membranes of low charge densities might be initiated at helix 1. The local binding information thus obtained gives a more differentiated picture of the affinity of \u03b1S to membranes. These findings contribute to our understanding of the details and structural consequences of \u03b1S\u2013membrane interactions.<\/jats:p>","DOI":"10.1002\/cbic.200800238","type":"journal-article","created":{"date-parts":[[2008,9,26]],"date-time":"2008-09-26T14:16:04Z","timestamp":1222438564000},"page":"2411-2416","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":57,"title":["Spin\u2010Label EPR on \u03b1\u2010Synuclein Reveals Differences in the Membrane Binding Affinity of the Two Antiparallel 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