New polyesterified triterpenes from the stems of <i>maesa membranacea</i> and their <i>α</i>-glucosidase inhibitory activities

A phytochemical investigation of the ethyl acetate extract from the stems of <i>Maesa membranacea</i> A. DC. resulted in the isolation of three polyesterified ursane-type triterpenes including two new derivatives (<b>1 </b>−<b> 2</b>), and one previously reported (<b>3</b>). Their chemical structures were determined based on the HR-ESI-MS and NMR spectroscopic data. In the <i>α</i>-glucosidase activity assay, MeOH extract of <i>M. membranacea</i> showed strong inhibition of the enzyme with an IC<sub>50</sub> value of 2.64 ± 0.06 μg/mL. Compounds <b>1</b> and <b>3</b> significantly inhibited <i>α</i>-glucosidase activity with IC<sub>50</sub> values of 25.39 ± 1.15 μg/mL and 21.71 ± 1.48 μg/mL, respectively. A molecular docking study of compounds <b>1</b> and <b>3</b> with <i>α</i>-glucosidase enzyme has suggested that these compounds bind to the enzyme at an allosteric site.

Publication Details

Journal
Figshare
Published
2025-01-01
DOI
https://doi.org/10.6084/m9.figshare.29634178.v1
Primary Topic
Natural product bioactivities and synthesis
Type
article
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article

New polyesterified triterpenes from the stems of maesa membranacea and their α-glucosidase inhibitory activities

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Natural product bioactivities and synthesis
article

New polyesterified triterpenes from the stems of maesa membranacea and their α-glucosidase inhibitory activities

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Abstract

A phytochemical investigation of the ethyl acetate extract from the stems of <i>Maesa membranacea</i> A. DC. resulted in the isolation of three polyesterified ursane-type triterpenes including two new derivatives (<b>1 </b>−<b> 2</b>), and one previously reported (<b>3</b>). Their chemical structures were determined based on the HR-ESI-MS and NMR spectroscopic data. In the <i>α</i>-glucosidase activity assay, MeOH extract of <i>M. membranacea</i> showed strong inhibition of the enzyme with an IC<sub>50</sub> value of 2.64 ± 0.06 μg/mL. Compounds <b>1</b> and <b>3</b> significantly inhibited <i>α</i>-glucosidase activity with IC<sub>50</sub> values of 25.39 ± 1.15 μg/mL and 21.71 ± 1.48 μg/mL, respectively. A molecular docking study of compounds <b>1</b> and <b>3</b> with <i>α</i>-glucosidase enzyme has suggested that these compounds bind to the enzyme at an allosteric site.

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Openalex Percentile: Top 61%
Natural product bioactivities and synthesis
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