Abstract
ABSTRACTIn this work, the binding of four hydroxyanthraquinones (HAQs) to fat mass and obesity-associated (FTO) protein has been studied using fluorescence, UV-vis absorption and circular dichroism spectroscopy as well as molecular docking analysis. Analysis of fluorescence data showed that the binding of HAQs to FTO occurred via a static quenching mechanism. Thermodynamic analysis and molecular docking results suggested that hydrophobic force played a major role in stabilising the HAQ-FTO complex. Circular dichroism spectra indicated that the secondary structure of FTO was changed by the addition of HAQs. Results also showed that emodin had the strongest quenching and binding ability among four HAQs.
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