Volume 51, Issue 7 pp. 1576-1579
Communication

Structural Basis of β-Amyloid-Dependent Synaptic Dysfunctions

Dr. Christian Haupt

Dr. Christian Haupt

Max Planck Research Unit for Enzymology of Protein Folding & MLU, Weinbergweg 22, 06120 Halle (Saale) (Germany)

These authors contributed equally to this work.

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Dr. Jörg Leppert

Dr. Jörg Leppert

Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)

These authors contributed equally to this work.

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Dr. Raik Rönicke

Dr. Raik Rönicke

DZNE-Standort Magdeburg c/o Leibniz-Institute for Neurobiology, Brenneckestrasse 6, 39118 Magdeburg (Germany)

These authors contributed equally to this work.

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Dr. Jessica Meinhardt

Dr. Jessica Meinhardt

Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)

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Dr. Jay K. Yadav

Dr. Jay K. Yadav

Max Planck Research Unit for Enzymology of Protein Folding & MLU, Weinbergweg 22, 06120 Halle (Saale) (Germany)

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Dr. Ramadurai Ramachandran

Dr. Ramadurai Ramachandran

Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)

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Dr. Oliver Ohlenschläger

Dr. Oliver Ohlenschläger

Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)

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Prof. Dr. Klaus G. Reymann

Prof. Dr. Klaus G. Reymann

DZNE-Standort Magdeburg c/o Leibniz-Institute for Neurobiology, Brenneckestrasse 6, 39118 Magdeburg (Germany)

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Dr. Matthias Görlach

Corresponding Author

Dr. Matthias Görlach

Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)

Matthias Görlach, Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)

Marcus Fändrich, Max Planck Research Unit for Enzymology of Protein Folding & MLU, Weinbergweg 22, 06120 Halle (Saale) (Germany)

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Priv.-Doz. Dr. Marcus Fändrich

Corresponding Author

Priv.-Doz. Dr. Marcus Fändrich

Max Planck Research Unit for Enzymology of Protein Folding & MLU, Weinbergweg 22, 06120 Halle (Saale) (Germany)

Matthias Görlach, Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)

Marcus Fändrich, Max Planck Research Unit for Enzymology of Protein Folding & MLU, Weinbergweg 22, 06120 Halle (Saale) (Germany)

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First published: 10 January 2012
Citations: 57

The authors thank K. Böhm for technical assistance. The Leibniz Institute for Age Research is financially supported by the State of Thuringia and the Federal Government of Germany. K.G.R. and M.F. are supported by the country Sachsen-Anhalt (Exzellenznetzwerk Biowissenschaften). M.F. was additionally supported by grants from the DFG (SFB 610) and the BMBF (BioFuture).

Graphical Abstract

Learn about Alzheimer: The molecular conformation of a toxic β-amyloid oligomer structure was determined by NMR spectroscopy (see picture). The measurements show a N-terminal β strand that controls the partitioning between oligomer and protofibril formation. Targeting the N-terminus of the peptide neutralizes Aβ-dependent neuronal dysfunctions. The data have important implications for understanding the structural basis of Alzheimer's disease.

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