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Binding of Filamentous Actin and Winding into Fibrillar Aggregates by the Polyphenolic C‐Glucosidic Ellagitannin Vescalagin
Author(s) -
Quideau Stéphane,
DouatCasassus Céline,
Delannoy López Daniela Melanie,
Di Primo Carmelo,
Chassaing Stefan,
Jacquet Rémi,
Saltel Frédéric,
Genot Elisabeth
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201006712
Subject(s) - actin , polyphenol , ellagitannin , chemistry , cytoskeleton , actin cytoskeleton , biophysics , actin binding protein , microbiology and biotechnology , biochemistry , biology , cell , antioxidant
Winding it up : The plant polyphenolic metabolite vescalagin fulfills all the requirements for use as an antiactin agent in cellular biological investigations. Despite its high hydrophilicity, it rapidly enters cells and disturbs the organization of the actin cytoskeleton in a dose‐dependent reversible manner by binding fibrillar actin and forcing the actin filaments (left) to wind themselves into ball‐like fibrillar aggregates (right).