These authors contributed equally.
Binding of Filamentous Actin and Winding into Fibrillar Aggregates by the Polyphenolic C-Glucosidic Ellagitannin Vescalagin†
Article first published online: 27 APR 2011
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 50, Issue 22, pages 5099–5104, May 23, 2011
How to Cite
Quideau, S., Douat-Casassus, C., Delannoy López, D. M., Di Primo, C., Chassaing, S., Jacquet, R., Saltel, F. and Genot, E. (2011), Binding of Filamentous Actin and Winding into Fibrillar Aggregates by the Polyphenolic C-Glucosidic Ellagitannin Vescalagin. Angew. Chem. Int. Ed., 50: 5099–5104. doi: 10.1002/anie.201006712
Financial support from the Agence Nationale de la Recherche (ANR-06-BLAN-0139 and ANR-06-BLAN-0362), the Conseil Regional d’Aquitaine (grant 20071301020), La Ligue Contre le Cancer (Comité Dordogne 2006 and 2007), and the Institut Européen de Chimie et Biologie (2007 Internal Seed Grant Program) is gratefully acknowledged. D.M.D.L. acknowledges the support of Fundayacucho and the French Embassy in Caracas, Venezuela, for her doctoral research assistantship. We thank A. Nube, A. Labrousse, and I. Maridonneau-Parini for preliminary experiments, R. Boujemaa-Paterski and L. Blanchoin for reagents and precious advice on actin polymerization assays, and A. Grelard for NMR spectroscopic experiments.
- Issue published online: 16 MAY 2011
- Article first published online: 27 APR 2011
- Manuscript Revised: 23 DEC 2010
- Manuscript Received: 26 OCT 2010
- Agence Nationale de la Recherche. Grant Numbers: ANR-06-BLAN-0139, ANR-06-BLAN-0362
- Conseil Regional d’Aquitaine. Grant Number: 20071301020
- La Ligue Contre le Cancer
- Institut Européen de Chimie et Biologie
- natural products;
- surface plasmon resonance
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).