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Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water

Authors

  • Hai-Young Kim,

    1. Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen (Germany), Fax: (+49) 551-201-2202
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  • Min-Kyu Cho,

    1. Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen (Germany), Fax: (+49) 551-201-2202
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  • Dietmar Riedel Dr.,

    1. Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen (Germany), Fax: (+49) 551-201-2202
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  • Claudio O. Fernandez Dr.,

    1. Instituto de Biología Molecular y Celular de Rosario, Universidad Nacional de Rosario, Suipacha 531, S2002 LRK Rosario (Argentina)
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  • Markus Zweckstetter Dr.

    1. Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen (Germany), Fax: (+49) 551-201-2202
    2. DFG Research Center for the Molecular Physiology of the Brain, 37077 Goettingen (Germany)
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  • We thank Prof. Dr. Christian Griesinger for discussions and Dr. Stefan Becker for help with protein production. This work was supported by a DFG-Graduiertenkolleg (GRK782) scholarship to M.-K.C., a DFG Heisenberg grant (ZW 71/2-1 & 3-1) to M.Z., the Alexander von Humboldt Foundation (Follow up Program), and by the Max Planck society.

Abstract

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Out in the cold: Amyloid fibrils formed by the protein α-synuclein, one of the key players in Parkinson's disease, are rapidly dissociated in supercooled water at −15 °C (see TEM images), conditions in which many globular proteins remain folded. NMR studies indicate that the weakening of hydrophobic and electrostatic interactions contribute to the cold-induced destabilization of the amyloid fibrils.

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