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Spin-Label EPR on alpha-Synuclein Reveals Differences in the Membrane Binding Affinity of the Two Antiparallel Helices

Spin-Label EPR on alpha-Synuclein Reveals Differences in the Membrane Binding Affinity of the Two Antiparallel Helices

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DRESCHER, Malte, Frans GODSCHALK, Gertjan VELDHUIS, Bart D. van ROOIJEN, Vinod SUBRAMANIAM, Martina HUBER, 2008. Spin-Label EPR on alpha-Synuclein Reveals Differences in the Membrane Binding Affinity of the Two Antiparallel Helices. In: ChemBioChem. 9(15), pp. 2411-2416. ISSN 1439-4227. eISSN 1439-7633

@article{Drescher2008Spin--1043, title={Spin-Label EPR on alpha-Synuclein Reveals Differences in the Membrane Binding Affinity of the Two Antiparallel Helices}, year={2008}, doi={10.1002/cbic.200800238}, number={15}, volume={9}, issn={1439-4227}, journal={ChemBioChem}, pages={2411--2416}, author={Drescher, Malte and Godschalk, Frans and Veldhuis, Gertjan and Rooijen, Bart D. van and Subramaniam, Vinod and Huber, Martina} }

Subramaniam, Vinod 2008 Subramaniam, Vinod Huber, Martina Godschalk, Frans The putative function of the Parkinson's disease-related protein -Synuclein (S) is thought to involve membrane binding. Therefore, the interaction of S 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 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 S140 resulted in two mobility components with correlation times of 0.5 and 3 ns, for POPG mole fractions >0.4. Monitoring these components as a function of the POPG mole fraction revealed that at low negative-charge densities helix 1 is more tightly bound than helix 2; this indicates a partially bound form of S. Thus, the interaction of 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 S to membranes. These findings contribute to our understanding of the details and structural consequences of S-membrane interactions. Spin-Label EPR on alpha-Synuclein Reveals Differences in the Membrane Binding Affinity of the Two Antiparallel Helices Publ. in: ChemBioChem 9 (2008), 15, pp. 2411-2416 Godschalk, Frans Veldhuis, Gertjan Huber, Martina Rooijen, Bart D. van deposit-license Drescher, Malte Veldhuis, Gertjan eng 2011-03-22T17:54:56Z Rooijen, Bart D. van Drescher, Malte 2011-03-22T17:54:56Z

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