Inhibitory effects of phenolic glycosides from <i>Trollius chinensis</i> Bunge on α-glucosidase: inhibition kinetics and mechanisms
Jie Feng, Fengming He, Yuhui Huang, Mi Zhou, Xiangzhong Liu, Xiansheng Ye, Renjing Yang, Wenjing Tian, Haifeng Chen
Abstract
value of 3.14 μM. Analysis of synchronous fluorescence and circular dichroism spectroscopy indicated that the binding of 1 to α-glucosidase led to the rearrangement and conformational alteration of the α-glucosidase enzyme. Furthermore, molecular docking indicated that 1 had a high affinity close to the active site pocket of α-glucosidase and indirectly inhibited the catalytic activity of the enzyme. However, 3 was bound to the entrance part of the active center of α-glucosidase and could hinder the release of the substrate as well as the catalytic reaction product, eventually suppressing the catalytic activity of α-glucosidase.