Multispectral and Molecular Dynamics Study on the Interactions Between α-Amylase and Four Sesquiterpene Lactone Compounds

Abstract

This study compared the inhibitory effects and mechanisms of four sesquiterpene lactones derived from Asteraceae plants on α-amylase using enzymatic kinetics, multi-spectral techniques, and molecular docking methods. It was found that compounds A, B, and C inhibited α-amylase activity through a competitive mechanism, while compound D exhibited non-competitive inhibition, with compound B showing the strongest inhibitory activity. Further analysis revealed that the four sesquiterpene lactone compounds interacted with key amino acid residues of α-amylase via hydrogen bonding and hydrophobic interactions, forming stable protein–ligand complexes. Among them, compound B demonstrated the lowest binding energy, indicating the strongest binding affinity to α-amylase. By investigating the inhibitory effects of these sesquiterpene lactones with a common parent structure on α-amylase, the inhibitory mechanisms and potential pharmacophoric groups were elucidated, providing a scientific foundation for the development of antidiabetic functional foods and drugs based on sesquiterpene lactone scaffolds.