Analysis of inhibitory interaction between epigallocatechin gallate and alpha-glucosidase: A spectroscopy and...

Alpha-glucosidase is one of the main enzymes responsible for digesting starch. Inhibiting its activity is therefore being targeted as a strategy for tackling diabetes. Certain food components have the potential to act as natural α-glucosidase (SCG) inhibitors, such as the polyphenols found in tea. In this study, epigallocatechin gallate (EGCG) was shown to strongly inhibit SCG activity (IC₅₀ value = 3.7 × 10^-5 M). Multi-spectroscopic binding molecular simulations indicated that EGCG spontaneously bound to SCG through a combination of hydrogen bonding and hydrophobic interactions. The hypothesis was supported by the results from intrinsic fluorescence quenching, conformational change, surface hydrophobicity decrease, and molecular docking analysis of the SCG after binding. Molecular docking provided powerful visual insights into the nature of the molecular interactions involved. This research provides important new information about the interaction mechanism of EGCG and SCG, which may be beneficial to the development of functional foods to prevent diabetes.