The Polyphenol Piceid Destabilizes Preformed Amyloid Fibrils and Oligomers In Vitro: Hypothesis on Possible Molecular Mechanisms |
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Authors: | Céline Rivière Jean-Claude Delaunay Françoise Immel Christophe Cullin Jean-Pierre Monti |
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Institution: | (1) Laboratoire de physique et biophysique, GESVAB EA 3675, ISVV, Université de Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux cedex, France;(2) UMR 5095 CNRS, IBGC, Université Bordeaux 2, 1 rue Camille Saint Saens, 33077 Bordeaux cedex, France |
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Abstract: | Alzheimer’s disease (AD) is characterized by deposits of amyloid in various tissues. The neuronal cytotoxicity of Aβ 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 Aβ 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 Aβ that could open the hydrophobic zipper and shift the reversible equilibrium “random coil⇔β-sheet” to
the disordered structure. |
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Keywords: | Alzheimer’ s disease β -Amyloid Fibrils Oligomers Polyphenols |
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