Lignan Constituents from the Fruits of f. and Their α-Amylase, α-Glucosidase, and Protein Tyrosine Phosphatase 1B Inhibitory Activities.

Eight previously undescribed lignan glycosides, viburmacrosides A-H (-), and seven known analogues (-) were isolated from f. fruits through bioactivity-guided fractionation. Their structures and absolute configurations were elucidated by extensive spectroscopic analyses and chemical evidence. Using the well-recognized carbohydrate-hydrolyzing enzymes α-amylase and α-glucosidase, as well as the promising protein tyrosine phosphatase 1B (PTP1B), as inhibitory targets, all isolated compounds were tested for their antidiabetic potential . Compound displayed potent inhibitory activities with IC values of 9.9 ± 0.6 and 8.9 ± 0.5 μM against α-glucosidase and PTP1B, respectively. The enzymatic kinetics results suggested that compound competitively inhibited α-glucosidase while it suppressed α-amylase and PTP1B in the mixed-type manner. These findings supported that f. fruits may be a new functional food resource with antidiabetic potential.