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Cryogenic solid state NMR studies of fibrils of the Alzheimer’s disease amyloid-β peptide: perspectives for DNP

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Abstract

Dynamic Nuclear Polarization solid-state NMR holds the potential to enable a dramatic increase in sensitivity by exploiting the large magnetic moment of the electron. However, applications to biological solids are hampered in uniformly isotopically enriched biomacromolecules due to line broadening which yields a limited spectral resolution at cryogenic temperatures. We show here that high magnetic fields allow to overcome the broadening of resonance lines often experienced at liquid nitrogen temperatures. For a fibril sample of the Alzheimer’s disease β-amyloid peptide, we find similar line widths at low temperature and at room temperature. The presented results open new perspectives for structural investigations in the solid-state.

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Acknowledgments

This research was supported by the Helmholtz-Gemeinschaft, the Leibniz-Gemeinschaft and the DFG (Re1435, SFB449, SFB740). We are grateful to the Center for Integrated Protein Science Munich (CIPS-M) for financial support. J.M.L.d.A. acknowledges a postdoctoral stipend of the DFG (Lo1546). We thank Arne Linden for assistance in performing the DNP experiments at the Leibniz-Institut für Molekulare Pharmakologie (FMP), and Antoine Loquet, Max-Planck-Institut für Biophysikalische Chemie in Göttingen, for assitance in the low temperature measurements at 850 MHz.

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Correspondence to Bernd Reif.

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Lopez del Amo, JM., Schneider, D., Loquet, A. et al. Cryogenic solid state NMR studies of fibrils of the Alzheimer’s disease amyloid-β peptide: perspectives for DNP. J Biomol NMR 56, 359–363 (2013). https://doi.org/10.1007/s10858-013-9755-5

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