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...
Saved in:
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Taylor & Francis Group
2025-12-01
|
| Series: | Journal of Enzyme Inhibition and Medicinal Chemistry |
| Subjects: | |
| Online Access: | https://www.tandfonline.com/doi/10.1080/14756366.2025.2492706 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850171592229781504 |
|---|---|
| author | Viruska Jaichand Adedayo Ayodeji Lanrewaju Himansu Baijnath Saheed Sabiu Viresh Mohanlall |
| author_facet | Viruska Jaichand Adedayo Ayodeji Lanrewaju Himansu Baijnath Saheed Sabiu Viresh Mohanlall |
| author_sort | Viruska Jaichand |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-6f0d5e1cb6be4f928a8bc626425f3341 |
| institution | OA Journals |
| issn | 1475-6366 1475-6374 |
| language | English |
| publishDate | 2025-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Journal of Enzyme Inhibition and Medicinal Chemistry |
| spelling | doaj-art-6f0d5e1cb6be4f928a8bc626425f33412025-08-20T02:20:15ZengTaylor & Francis GroupJournal of Enzyme Inhibition and Medicinal Chemistry1475-63661475-63742025-12-0140110.1080/14756366.2025.2492706Profiling and cheminformatics bioprospection of curcurbitacin I and momordin Ic from Momordica balsamina on α-amylase and α-glucosidaseViruska Jaichand0Adedayo Ayodeji Lanrewaju1Himansu Baijnath2Saheed Sabiu3Viresh Mohanlall4Department of Biotechnology and Food Science, Faculty of Applied Science, Durban University of Technology, Durban, South AfricaDepartment of Biotechnology and Food Science, Faculty of Applied Science, Durban University of Technology, Durban, South AfricaWard Herbarium, School of Life Sciences, University of KwaZulu-Natal, Durban, South AfricaDepartment of Biotechnology and Food Science, Faculty of Applied Science, Durban University of Technology, Durban, South AfricaDepartment of Biotechnology and Food Science, Faculty of Applied Science, Durban University of Technology, Durban, South AfricaMomordica 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.https://www.tandfonline.com/doi/10.1080/14756366.2025.2492706Binding free energycucurbitacin IMomordica balsaminamomordin Ictype 2 diabetes mellitus |
| spellingShingle | Viruska Jaichand Adedayo Ayodeji Lanrewaju Himansu Baijnath Saheed Sabiu Viresh Mohanlall Profiling and cheminformatics bioprospection of curcurbitacin I and momordin Ic from Momordica balsamina on α-amylase and α-glucosidase Journal of Enzyme Inhibition and Medicinal Chemistry Binding free energy cucurbitacin I Momordica balsamina momordin Ic type 2 diabetes mellitus |
| title | Profiling and cheminformatics bioprospection of curcurbitacin I and momordin Ic from Momordica balsamina on α-amylase and α-glucosidase |
| title_full | Profiling and cheminformatics bioprospection of curcurbitacin I and momordin Ic from Momordica balsamina on α-amylase and α-glucosidase |
| title_fullStr | Profiling and cheminformatics bioprospection of curcurbitacin I and momordin Ic from Momordica balsamina on α-amylase and α-glucosidase |
| title_full_unstemmed | Profiling and cheminformatics bioprospection of curcurbitacin I and momordin Ic from Momordica balsamina on α-amylase and α-glucosidase |
| title_short | Profiling and cheminformatics bioprospection of curcurbitacin I and momordin Ic from Momordica balsamina on α-amylase and α-glucosidase |
| title_sort | profiling and cheminformatics bioprospection of curcurbitacin i and momordin ic from momordica balsamina on α amylase and α glucosidase |
| topic | Binding free energy cucurbitacin I Momordica balsamina momordin Ic type 2 diabetes mellitus |
| url | https://www.tandfonline.com/doi/10.1080/14756366.2025.2492706 |
| work_keys_str_mv | AT viruskajaichand profilingandcheminformaticsbioprospectionofcurcurbitaciniandmomordinicfrommomordicabalsaminaonaamylaseandaglucosidase AT adedayoayodejilanrewaju profilingandcheminformaticsbioprospectionofcurcurbitaciniandmomordinicfrommomordicabalsaminaonaamylaseandaglucosidase AT himansubaijnath profilingandcheminformaticsbioprospectionofcurcurbitaciniandmomordinicfrommomordicabalsaminaonaamylaseandaglucosidase AT saheedsabiu profilingandcheminformaticsbioprospectionofcurcurbitaciniandmomordinicfrommomordicabalsaminaonaamylaseandaglucosidase AT vireshmohanlall profilingandcheminformaticsbioprospectionofcurcurbitaciniandmomordinicfrommomordicabalsaminaonaamylaseandaglucosidase |