Abstract:1-Deoxynojirimycin (DNJ) is a natural alkaloid found in mulberry leaf, which can significantly delay the degradation process of polysaccharides as a potent glycemic enzyme due to similar to the structure of glucose. This experiment identified the targets of DNJ and clarified their action models from PTP1B, PPAR alpha, PPAR gamma, alpha Amylase (alpha Amylase) and alpha glycosidase enzymes (alpha - glucosidase) in protein by the molecular docking and molecular dynamics simulation method. The results showed that the alpha -glucosidase had absolute advantages to bind DNJ, further analysis of the hydrogen bond and the decomposition results showed that the Glu268, Asp330 and Asp199 were the key residues, which played an important role in the combination of DNJ and alpha Glucosidase. Its function was to form stable hydrogen bonds, and electrostatic force and polar solvation were the main sources of binding force. DNJ played the role of hypoglycemia by inhibiting the bioactivity of alpha glucosidase through combination with the above residues. The study illustrated the action mode of DNJ and alpha - glucosidase from the molecular structure level, which provided a clue to rational drug design and virtual screening of small molecule database based on the structure of DNJ.
