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Updated: Jun 27, 2026

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
Published on: May 22, 2018
The polyphenol piceid destabilizes preformed amyloid fibrils and oligomers in vitro: hypothesis on possible molecular
Céline Rivière1, Jean-Claude Delaunay, Françoise Immel
1Laboratoire de physique et biophysique, GESVAB EA 3675, ISVV, Université de Bordeaux 2, Bordeaux cedex, France.
Abstract:
Alzheimer's disease (AD) is characterized by deposits of amyloid in various tissues. The neuronal cytotoxicity of Abeta peptides is attributed not only to various mechanisms but also to amyloid fibrils and soluble oligomeric intermediates. Consequently, finding molecules to prevent or reverse the oligomerization and fibrillization of Abeta could be of therapeutic value in the treatment of AD. We show that piceid, a polyphenol of the stilbene family, destabilized fibrils and oligomers to give back monomers that are not neurotoxic molecules. The mechanism of this destabilization could be a dynamic interaction between the polyphenol and the Abeta that could open the hydrophobic zipper and shift the reversible equilibrium "random coil<-->beta-sheet" to the disordered structure.
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