Structural characterization and α-glycosidase inhibitory activity of a novel polysaccharide fraction from Aconitum coreanum

Carbohydr Polym. 2020 Feb 15:230:115586. doi: 10.1016/j.carbpol.2019.115586. Epub 2019 Nov 9.

Abstract

α-Glycosidase is an essential target for the management of postprandial serum glucose in diabetic patients. Therefore, the interest has been growing in the screening of α-glycosidase inhibitor from natural resource. In the present study, the structure and α-glycosidase inhibitory activity of a polysaccharide (named as ACPP-1) from Aconitum coreanum were investigated. Based on the results from high performance gel permeation chromatography, GC-MS and 1D/2D nuclear magnetic resonance spectroscopy, ACPP-1 was a highly-linear polysaccharide with a molecular weight of 34.0 kD and containing over 90 % of glucose. It was composed of (1→4)-α-d-Glcp and α-Araf. ACPP-1 exhibited a dose-dependent inhibitory eff ;ect against α-glycosidase activity in vitro and the IC50 value was ∼0.8 mg/mL. In oral starch tolerance test, treatment with ACPP-1 (800 mg/kg) significantly improved the starch tolerance in mice. Taken together, this study provided a potential intervention and management for postprandial hyperglycemia by the polysaccharide fraction from A. coreanum.

Keywords: A. coreanum polysaccharides (ACPP); Characterization; α-Glycosidase.

MeSH terms

  • Aconitum / chemistry*
  • Animals
  • Chromatography, Gel
  • Glycoside Hydrolase Inhibitors / chemistry*
  • Glycoside Hydrolase Inhibitors / pharmacology
  • Humans
  • Mice
  • Molecular Weight
  • Plant Extracts / chemistry
  • Plant Extracts / pharmacology
  • Polysaccharides / chemistry*
  • Polysaccharides / pharmacology
  • Polysaccharides / ultrastructure
  • alpha-Glucosidases / chemistry*
  • alpha-Glucosidases / pharmacology
  • alpha-Glucosidases / ultrastructure

Substances

  • Glycoside Hydrolase Inhibitors
  • Plant Extracts
  • Polysaccharides
  • alpha-Glucosidases