Quercetin and other flavonoids bind to actin and affect its biological activity

In a screen for flavonoid target proteins we identified actin as a quercetin-binding protein. This interaction was studied using fluorescence and infrared spectroscopy and compared with the binding parameters of related flavonoids. The biological relevance of the flavonoid/actin interaction in the cytoplasm and the nucleus was assayed using an actin polymerization and a transcription assay, respectively. While some flavonols inhibit actin functions, the structurally related epigallocatechin tends to promote actin functions in the chosen in vitro assays. Furthermore, cellular test systems were used to evaluate the biological consequences of the flavonoid/actin interaction. The flavonoid – induced conformational changes of actin were analyzed by infrared spectroscopy. The obtained data and in silico docking studies gave further insights into possible modes of protein-ligand interactions and helped to understand the molecular basis of the observed biological effects.