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

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.