Coumarins from Seseli petraeum M. Bieb. (Apiaceae) and their α-glucosidase inhibitory activity


ÖNDER A., Cinar A. S., Baran M. Y., Kuruuzum-Uz A., Trendafilova A.

South African Journal of Botany, vol.144, pp.458-463, 2022 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 144
  • Publication Date: 2022
  • Doi Number: 10.1016/j.sajb.2021.09.022
  • Journal Name: South African Journal of Botany
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Geobase, Veterinary Science Database
  • Page Numbers: pp.458-463
  • Keywords: Apiaceae, coumarins, Seseli, Seseli petraeum, alpha-amylase, alpha-glucosidase, ANGULAR-TYPE PYRANOCOUMARINS, CONSTITUENTS, SEPARATION, PLANTS
  • Lokman Hekim University Affiliated: Yes

Abstract

© 2021 SAABSeseli L. species from the Apiaceae family are well-known medicinal plants with rich bioactive components. In the present study, the phytochemical investigation of the n-hexane extract of the aerial parts from Seseli petraeum M. Bieb., a fairly narrow growing plant on the northern side of Turkey, led to the isolation of one new pyranocoumarin called 3′-isovaleryl-4′-oxo-lomatin (petracoumarin, (1) along with 12 known coumarins octanoyllomatin (2), selinidin (3), anomalin (4), 3′-isobutryl-lomatin (5), 3′-angeloyl-4′-isovaleryl-cis-khellactone (6), 3′-isovaleryl-4′-angeloyl-cis-khellactone (7), calipteryxin (8), samidin (9), 4′-senecioyl-cis-khellactone (10), 3′-senecioyl-cis-khellactone (11), cis-khellactone (12) and angelicin (13), and six plant sterols (campesterol, stigmasterol, β-sitosterol, stigmastanol, stigma-7-en-3-ol and γ-ergosterol, 14–19). The structures of the coumarins were elucidated by spectroscopic methods, including extensive 1D/2D NMR, and MS techniques. In addition, several coumarins have been tested for their inhibitory activity against α-amylase and α-glucosidase enzymes. The coumarins exhibited notable inhibitory activity against the α-glucosidase enzyme and low inhibitory potential against α-amylase. Among the tested compounds, octanoyllomatin (2) was found to be the best inhibitor of α-glucosidase with IC50 = 69.00 ± 0.43 µg/mL. The promising results will guide our future studies and suggest that more detailed studies can be done on in vivo models.