Identification of Pinocembrin as an Anti-Glycation Agent and α-Glucosidase Inhibitor from Fingerroot (Boesenbergia rotunda): The tentative structure–activity relationship towards Mg-trapping activity

Thammatee Potipiranun, Sirichai Adisakwattana, Wisuttaya Worawalai, Rico Ramadhan, Preecha Phuwapraisirisan

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)

Abstract

Diabetes mellitus (DM) is a disease that is caused by a malfunction of carbohydrate metabolism, which plays an important role in the development of long-term diabetic complications. The excess glucose can be transformed to methylglyoxal (MG), a potential precursor of glycation. Glycation is a spontaneous non-enzymatic reaction that initially yields advanced glycation end-products (AGEs), which ultimately triggers several severe complications. Therefore, the inhibition of AGEs formation is the imperative approach for alleviating diabetic complications. The aim of this research was to investigate the glycation and α-glucosidase inhibitory abilities of compounds isolated from fingerroot. The dichloromethane extract afforded three flavanones, two chalcones, two dihydrochalcones, and one kavalactone. Most of the isolated compounds showed higher inhibition effect against AGEs formation than aminoguanidine (AG). Subsequent evaluation in MG-trapping assay indicated that their trapping potency was relatively comparable to AG. Their structure-activity relationships (SAR) of MG-trapping activity were investigated using the comparison of the structures of flavonoids. In addition, pinocembrin displayed moderate α-glucosidase inhibition against both maltase and sucrose, with IC50 values of 0.35 ± 0.021 and 0.39 ± 0.020 mM, respectively.

Original languageEnglish
Article number3365
JournalMolecules
Volume23
Issue number12
DOIs
Publication statusPublished - 19 Dec 2018

Keywords

  • Advanced glycation end-products
  • Boesenbergia rotunda
  • Diabetes
  • Methylglyoxal
  • Pinocembrin
  • Structure-activity relationship
  • α-glucosidase

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