Alpha-glucosidase and tyrosinase inhibiton of polyphenols isolated from Potentilla speciosa var. speciosa: In vitro and in silico perspectives

Özgünseven A., BARUT B., Šoral M., SARI S., AKAYDIN G., ÖZEL A., ...Daha Fazla

Industrial Crops and Products, cilt.170, 2021 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 170
  • Basım Tarihi: 2021
  • Doi Numarası: 10.1016/j.indcrop.2021.113806
  • Dergi Adı: Industrial Crops and Products
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aerospace Database, Biotechnology Research Abstracts, CAB Abstracts, Communication Abstracts, Food Science & Technology Abstracts, INSPEC, Metadex, Veterinary Science Database
  • Anahtar Kelimeler: Cinnamtannin D1, Potentilla, Rosaceae, Molecular modelling, MECHANISTIC INSIGHTS, RHODODENDRON-FORMOSANUM, KINETICS, DOCKING, IDENTIFICATION, PROCYANIDINS, METABOLITE, FLAVONOIDS, QUERCETIN, DISCOVERY
  • Hacettepe Üniversitesi Adresli: Evet

Özet

© 2021 Elsevier B.V.In order to explore the antidiabetic and anti-pigmentation potential of Potentilla species, which have been used for the treatment of diabetes and some skin problems, α-glucosidase and tyrosinase inhibitory effects of Potentilla speciosa Willd. var. speciosa Willd. were tested. The n-butanol extract showed significant α-glucosidase inhibition (IC50 = 3.08 ± 0.48 ppm). Phytochemical studies on this extract led to isolation of catechin, miquelianin, tiliroside, and cinnamtannin D1, the occurrence of the latter in the genus Potentilla is reported for the first time in this study. Miquelianin showed the highest inhibitory effect on tyrosinase with an IC50 value of 86.60 ± 1.90 μM. Cinnamtannin D1 emerged as an excellent α-glucosidase inhibitor with an IC50 value (0.849 ± 0.014 μM), approximately 53 times higher than the value of the positive control, acarbose. It was found to inhibit α-glucosidase in a noncompetitive manner with a Ki value of 0.240 ± 0.010 μM. Molecular modeling studies showed that cinnamtannin D1 most likely bound to an allosteric site of the enzyme.