Journal
FOOD & FUNCTION
Volume 13, Issue 5, Pages 2857-2864Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1fo03347f
Keywords
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Funding
- Natural Science Foundation of China [81773866, U1605221, 81602988]
- Fundamental Research Funds for the Central Universities [20720190079]
- Natural Science Foundation of Fujian Province of China [2019J007]
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Two undescribed phenolic glycosides were isolated from the Trollius chinensis Bunge plant, showing different inhibitory effects on alpha-glucosidase. Spectroscopic analysis revealed the structural changes of the enzyme during binding with these compounds.
Two undescribed phenolic glycosides, trochinenols B and C (1 and 2), together with four known analogues (3-6), were isolated from the functional tea Trollius chinensis Bunge and their alpha-glucosidase inhibitory kinetics and mechanisms were investigated. It was found that 1 inhibited alpha-glucosidase in a noncompetitive manner with an IC50 value of 25.96 mu M, while 3 showed a notable inhibitory effect against alpha-glucosidase in an uncompetitive manner with an IC50 value of 3.14 mu M. Analysis of synchronous fluorescence and circular dichroism spectroscopy indicated that the binding of 1 to alpha-glucosidase led to the rearrangement and conformational alteration of the alpha-glucosidase enzyme. Furthermore, molecular docking indicated that 1 had a high affinity close to the active site pocket of alpha-glucosidase and indirectly inhibited the catalytic activity of the enzyme. However, 3 was bound to the entrance part of the active center of alpha-glucosidase and could hinder the release of the substrate as well as the catalytic reaction product, eventually suppressing the catalytic activity of alpha-glucosidase.
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