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The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.

Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compounds

Caruana, Mario, Högen, Tobias, Levin, Johannes, Hillmer, Andreas, Giese, Armin, Vassallo, Neville·2011·FEBS Letters

Abstract

Aggregation of alpha-synuclein (αS) into oligomers is critically involved in the pathogenesis of Parkinson's disease (PD). Using confocal single-molecule fluorescence spectroscopy, we have studied the effects of 14 naturally-occurring polyphenolic compounds and black tea extract on αS oligomer formation. We found that a selected group of polyphenols exhibited potent dose-dependent inhibitory activity on αS aggregation. Moreover, they were also capable of robustly disaggregating pre-formed αS oligomers. Based upon structure-activity analysis, we propose that the key molecular scaffold most effective in inhibiting and destabilizing self-assembly by αS requires: (i) aromatic elements for binding to the αS monomer/oligomer and (ii) vicinal hydroxyl groups present on a single phenyl ring. These findings may guide the design of novel therapeutic drugs in PD.

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Metadata

Authors
Caruana, M., Högen, T., Levin, J., Hillmer, A., Giese, A., & Vassallo, N.
Venue
FEBS Letters
Publisher
Wiley
Published
2011-03-26
Volume
585
Issue
8
Pages
1113-1120
ISSN
0014-5793 (ISSN-L)
OpenAlex
W2038828761
Cited by
273
References
41
FWCI
7.68
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compounds. https://app.cochat.ai/papers/10.1016/j.febslet.2011.03.046
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Caruana, M., Högen, T., Levin, J., Hillmer, A., Giese, A., & Vassallo, N. (2011). Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compounds. FEBS Letters. https://doi.org/10.1016/j.febslet.2011.03.046

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