Binding of Filamentous Actin and Winding into Fibrillar Aggregates by the Polyphenolic C-Glueosidic Ellagitanein Vescalagin

摘要

Herein we describe the effects of the C-glucosidic ellagitannin vescalagin (1, Figure 1 a), a polyphenolic natural product readily available from fagaceous woody plant sources, such as oak (Quercus sp.), on actin, one of the most abundant structural proteins in eukaryotic cells. Monomeric globular actin (G-actin) subunits assemble through an adenosine triphosphate (ATP) dependent process into polymeric fibrillar actin (F-actin) filaments, which are further ordered into three-dimensional architectures to establish the functional actin cytoskeleton. A dynamic equilibrium between the G-actin and F-actin states continuously ensures the adaptation of the actin cytoskeleton during its various roles in controlling cell shape, cytokinesis, motility, adhesion, and gene expression.