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.
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Communication
Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water†
Article first published online: 2 JUN 2008
DOI: 10.1002/anie.200800342
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Kim, H.-Y., Cho, M.-K., Riedel, D., Fernandez, Claudio O. and Zweckstetter, M. (2008), Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water. Angew. Chem. Int. Ed., 47: 5046–5048. doi: 10.1002/anie.200800342
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Publication History
- Issue published online: 16 JUN 2008
- Article first published online: 2 JUN 2008
- Manuscript Received: 22 JAN 2008
Keywords:
- α-synuclein;
- amyloid fibrils;
- electron microscopy;
- NMR spectroscopy;
- proteins
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.