Study of the Interaction between ZnO@rGO Loaded with Formononetin and α-Glucosidase
The interaction between ZnO@rGO loaded formononetin(For)and α-glucosidase(α-Glu)was studied by UV-Vis spectrometry,fluorescence spectroscopy,circular dichroism and enzyme inhibition kinetics.For was found to adsorb on the surface of ZnO@rGO by π-π stacking to form a complex.Fluorescence quenching showed that the binding constant between For and α-Glu increased in the presence of ZnO@rGO,and the interaction forces were hydrogen bonding and van der Waals forces.A study on the inhibition kinetics of α-Glu further showed that α-Glu-For belonged to competitive inhibition,α-Glu-ZnO@rGO-For belonged to anti-competitive inhibition,and its inhibition constants Ki.For＞Kis,ZnO@rGO-For,indicating that ZnO@rGO-For had a greater inhibitory effect on α-Glu than pure For.Circular dichroism confirmed that ZnO@rGO had little effect on the conformation of α-Glu.The comprehensive study provides useful information for the study of ZnO@rGO as a drug carrier,and also offers new ideas for the treatment of diabetes.
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