Piceatannol and Other Wine Stilbenes: A Pool of Inhibitors against α-Synuclein Aggregation and Cytotoxicity

Nutrients. 2016 Jun 15;8(6):367. doi: 10.3390/nu8060367.

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.

Keywords: Parkinson’s disease; piceatannol; stilbene; α-synuclein.

MeSH terms

  • Animals
  • Benzothiazoles
  • Cell Survival / drug effects
  • Electrophoresis, Polyacrylamide Gel
  • Flavonoids / pharmacology
  • Microscopy, Electron, Transmission
  • PC12 Cells
  • Parkinson Disease / drug therapy
  • Rats
  • Stilbenes / pharmacology*
  • Thiazoles
  • Wine / analysis*
  • alpha-Synuclein / antagonists & inhibitors
  • alpha-Synuclein / toxicity*

Substances

  • Benzothiazoles
  • Flavonoids
  • Stilbenes
  • Thiazoles
  • alpha-Synuclein
  • hopeaphenol
  • thioflavin T
  • ampelopsin
  • 3,3',4,5'-tetrahydroxystilbene