Nutrients 2016, 8(6), 367; https://doi.org/10.3390/nu8060367
Piceatannol and Other Wine Stilbenes: A Pool of Inhibitors against α-Synuclein Aggregation and Cytotoxicity
1
Université de Bordeaux, ISVV, EA 4577 Oenologie, Faculté de Pharmacie, MIB (GESVAB), Villenave d’Ornon 33882, France
2
INRA, ISVV, USC 1366 Oenologie, Villenave d’Ornon 33882, France
3
CBMN-UMR 5248 CNRS, Université de Bordeaux, IPB, Allée Geoffroy St. Hilaire, Pessac 33600, France
*
Author to whom correspondence should be addressed.
Received: 15 February 2016 / Revised: 12 May 2016 / Accepted: 1 June 2016 / Published: 15 June 2016
(This article belongs to the Special Issue Selected Papers from Resveratrol Regional Meeting 2015)
Abstract
The aggregation of α-synuclein is one on the key pathogenic events in Parkinson’s disease. In the present study, we investigated the inhibitory capacities of stilbenes against α-synuclein aggregation and toxicity. Thioflavin T fluorescence, transmission electronic microscopy, and SDS-PAGE analysis were performed to investigate the inhibitory effects of three stilbenes against α-synuclein aggregation: piceatannol, ampelopsin A, and isohopeaphenol. Lipid vesicle permeabilization assays were performed to screen stilbenes for protection against membrane damage induced by aggregated α-synuclein. The viability of PC12 cells was examined using an MTT assay to assess the preventive effects of stilbenes against α-synuclein-induced toxicity. Piceatannol inhibited the formation of α synuclein fibrils and was able to destabilize preformed filaments. It seems to induce the formation of small soluble complexes protecting membranes against α-synuclein-induced damage. Finally, piceatannol protected cells against α-synuclein-induced toxicity. The oligomers tested (ampelopsin A and hopeaphenol) were less active. View Full-TextKeywords:
stilbene; piceatannol; Parkinson’s disease; α-synuclein
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Temsamani, H.; Krisa, S.; Decossas-Mendoza, M.; Lambert, O.; Mérillon, J.-M.; Richard, T. Piceatannol and Other Wine Stilbenes: A Pool of Inhibitors against α-Synuclein Aggregation and Cytotoxicity. Nutrients 2016, 8, 367.
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