Profiling and cheminformatics bioprospection of curcurbitacin I and momordin Ic from Momordica balsamina on α-amylase and α-glucosidase
Momordica spp. has been traditionally used to manage type 2 diabetes mellitus, but the mechanisms and metabolites remain unclear. This study evaluated the inhibitory potential of Momordica balsamina extracts on α-amylase and α-glucosidase in vitro, identifying cucurbitacin I and momordin Ic via high...
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| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Taylor & Francis Group
2025-12-01
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| Series: | Journal of Enzyme Inhibition and Medicinal Chemistry |
| Subjects: | |
| Online Access: | https://www.tandfonline.com/doi/10.1080/14756366.2025.2492706 |
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| Summary: | Momordica spp. has been traditionally used to manage type 2 diabetes mellitus, but the mechanisms and metabolites remain unclear. This study evaluated the inhibitory potential of Momordica balsamina extracts on α-amylase and α-glucosidase in vitro, identifying cucurbitacin I and momordin Ic via high-performance liquid chromatography-photo diode array, and their inhibitory potential in silico. Ethyl acetate seed extract (14.46 µg/ml) and hexane fruit flesh extract (16.79 µg/ml) exhibited lower IC50 values against α-amylase and α-glucosidase, respectively, compared to acarbose (reference standard). Comparatively, momordin Ic concentrations (36.57–605.98 µg/ml) were higher than cucurbitacin I (17.08–44.34 µg/ml). A 140 ns simulation showed that cucurbitacin I (−63.06 kcal/mol) and momordin Ic (−66.53 kcal/mol) exhibited stronger binding to α-amylase than acarbose (−36.46 kcal/mol), whereas cucurbitacin I (−38.08 kcal/mol) and momordin Ic (−54.87 kcal/mol) displayed weaker binding to α-glucosidase, relative to acarbose (−63.73 kcal/mol). Generally, momordin Ic demonstrated better thermodynamic properties, hence further in vitro and in vivo studies are needed to validate their antidiabetic potential. |
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| ISSN: | 1475-6366 1475-6374 |