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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-B1DE-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0001-20E4-9
Genre: Journal Article

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 Creators:
Fonseca-Ornelas, L.1, Author              
Schmidt, C. D.2, Author              
Camacho-Zarco, A. R.1, Author              
Fernandez, C. O.2, Author              
Becker, S.2, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: Alpha-synuclein; Mass spectrometry; Oligomerization; Small molecules
 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.

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Language(s): eng - English
 Dates: 2017-08-012017-09-21
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/chem.201703001
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Title: Chemistry. A European Journal
Source Genre: Journal
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Pages: - Volume / Issue: 23 (53) Sequence Number: - Start / End Page: 13010 - 13014 Identifier: -