芦荟大黄素对α-葡萄糖苷酶的抑制机理及其与阿卡波糖的协同作用OA北大核心CSTPCD

In order to investigate the interaction between aloe emodin and α-glucosidase,enzyme kinetics,ultraviolet(UV)spectroscopy,infrared(IR)spectroscopy and fluorescence spectroscopy were employed to investigate the inhibitory mechanism of aloe emodin on α-glucosidase and the synergistic effect of aloe emodin in combination with acarbose was also investigated in this study.The results showed that aloe emodin had better inhibitory effect on α-glucosidase as both a non-competitive and anti-competitive inhibitor when compared with acarbose.The results of UV spectroscopy indicated that a new complex was formed through the interaction between aloe emodin and α-glucosidase.The characteristic vibrations of amide groups in the IR spectra indicated that the structural conformation of α-glucosidase changed with the addition of aloe emodin.The results of fluorescence quenching experiments showed that the endogenous fluorescence of α-glucosidase was statically quenched by aloe emodin.In addition,it was also found that aloe emodin combined with acarbose had a synergistic inhibitory effect on α-glucosidase activity.This study provides an experimental basis for the future application of aloe emodin in health foods for regulating blood glucose.