An investigation of the inhibitory mechanism of α-glucosidase by chysalodin from Aloe vera

The aim of our study is to provide new type skeleton of α-glucosidase inhibitor from food source. A new 6′-O-(E)–cinnamoyl-7-methoxy-aloin A (1) was isolated from Aloe vera. Also, known chysalodin (2) was the first report for A. vera. These structures were identified with based on HR-ESI Mass and 1/...

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Bibliographic Details
Published in:International journal of biological macromolecules 2020-03, Vol.147, p.314-318
Main Authors: Kim, Jang Hoon, Cho, Chong Woon, Lee, Jung In, Vinh, Le Ba, Kim, Kyung Tae, Cho, In Sook
Format: Article
Language:English
Subjects:
Aloe vera
Alpha-glucosidase
Competitive inhibitor
Fluorescence quenching
Xanthorrhoeaceae
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Summary:The aim of our study is to provide new type skeleton of α-glucosidase inhibitor from food source. A new 6′-O-(E)–cinnamoyl-7-methoxy-aloin A (1) was isolated from Aloe vera. Also, known chysalodin (2) was the first report for A. vera. These structures were identified with based on HR-ESI Mass and 1/2D-NMR spectra. These isolated compounds were tested for their inhibitory activities against α-glucosidase by using spectrophotometer. Of these, compound 2 exhibited inhibitory activity, with an IC50 value of 13.4 ± 1.5 μM. An enzyme kinetic study identified the mechanism of binding of the ligand with the enzyme; the ligand binds in the active site of the enzyme in a competitive mode. Additionally, fluorescence quenching between the ligand and receptor revealed a two-to-one reaction. Finally, this finding provides that anthraquinone dimer (2) could be a starting point for the design of new class of α-glucosidase inhibitor. •A new 6′-O-(E)–cinnamoyl-7-methoxy-aloin A (1), and chysalodin (2) were isolated from Aloe vera for the first time.•Chysalodin (2) was bound into α-glucosidase with IC50 value of 13.4 ± 1.5 μM.•Through steady-state kinetic study, this was revealed with competitive of mode for inhibition.•Fluorescence quenching led to calculate the kinetic parameters of compound 2.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2020.01.076