Estrogenic Activity of Sanguiin H-6 through Activation of Estrogen Receptor a Coactivator-binding Site

Abstract

A popular approach for the study of estrogen receptor a inhibition is to investigate the protein-protein interaction between the estrogen receptor (ER) and the coactivator surface. In our study, we investigated phytochemicals from Rubus coreanus that were able to disrupt ERa and coactivator interaction with an ERa antagonist. The E-screen assay and molecular docking analysis were performed to evaluate the effects of the estrogenic activity of R. coreanus extract and its constituents on the MCF-7 human breast cancer cell line. At 100 mg/mL, R. coreanus extract significantly stimulated cell proliferation (574.57 ? 8.56%). Sanguiin H6, which was isolated from R. coreanus, demonstrated the strongest affinity for the ERa coactivator-binding site in molecular docking analysis, with a binding energy of -250.149. The initial results of the study indicated that sanguiin H6 contributed to the estrogenic activity of R. coreanus through the activation of the ERa coactivator-binding site.