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Journal Article

Small molecule-induced soluble oligomers of α-synuclein with helical structure.

MPS-Authors
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Fonseca-Ornelas,  L.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Schmidt,  C. D.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Camacho-Zarco,  A. R.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Fernandez,  C. O.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

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2468397_Suppl.pdf
(Supplementary material), 4MB

Citation

Fonseca-Ornelas, L., Schmidt, C. D., Camacho-Zarco, A. R., Fernandez, C. O., Becker, S., & Zweckstetter, M. (2017). Small molecule-induced soluble oligomers of α-synuclein with helical structure. Chemistry. A European Journal, 23(53), 13010-13014. doi:10.1002/chem.201703001.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-B1DE-3
Abstract
Accumulation of α-synuclein (αSyn) aggregates constitutes the hallmark of synucleinopathies including Parkinson's disease. However, many steps from the innocuous, monomeric αSyn toward misfolded oligomers and fibrillar species remain unclear. Here, we show that αSyn can form in solution α-helical oligomers, which are off-pathway to fibrillization, through interaction with the tetrapyrrole phthalocyanine tetrasulfonate. Chemical cross-linking combined with mass spectrometry reveals a large number of intermolecular cross-links along the entire αSyn sequence in the phthalocyanine tetrasulfonate-stabilized αSyn oligomers. Our study suggests that stabilization of structured oligomers by small molecules provides a viable strategy to interfere with αSyn fibrillization.