Identification of Dipeptidyl Peptidase-4 and α-Amylase Inhibitors from <i>Melicope glabra</i> (Blume) T. G. Hartley (Rutaceae) Using Liquid Chromatography Tandem Mass Spectrometry, In Vitro and In Silico Methods
The present study investigated the antidiabetic properties of the extracts and fractions from leaves and stem bark of <i>M. glabra</i> based on dipeptidyl peptidase-4 (DPP-4) and α-Amylase inhibitory activity assays. The chloroform extract of the leaves was found to be most active toward...
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MDPI AG
2020-12-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/26/1/1 |
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| author | Alexandra Quek Nur Kartinee Kassim Amin Ismail Muhammad Alif Mohammad Latif Khozirah Shaari Dai Chuan Tan Pei Cee Lim |
| author_facet | Alexandra Quek Nur Kartinee Kassim Amin Ismail Muhammad Alif Mohammad Latif Khozirah Shaari Dai Chuan Tan Pei Cee Lim |
| author_sort | Alexandra Quek |
| collection | DOAJ |
| description | The present study investigated the antidiabetic properties of the extracts and fractions from leaves and stem bark of <i>M. glabra</i> based on dipeptidyl peptidase-4 (DPP-4) and α-Amylase inhibitory activity assays. The chloroform extract of the leaves was found to be most active towards inhibition of DPP-4 and α-Amylase with IC<sub>50</sub> of 169.40 μg/mL and 303.64 μg/mL, respectively. Bioassay-guided fractionation of the leaves’ chloroform extract revealed fraction 4 (CF4) as the most active fraction (DPP-4 IC<sub>50</sub>: 128.35 μg/mL; α-Amylase IC<sub>50</sub>: 170.19 μg/mL). LC-MS/MS investigation of CF4 led to the identification of trans-decursidinol (<b>1</b>), swermirin (<b>2</b>), methyl 3,4,5-trimethoxycinnamate (<b>3</b>), renifolin (<b>4</b>), 4′,5,6,7-tetramethoxy-flavone (<b>5</b>), isorhamnetin (<b>6</b>), quercetagetin-3,4′-dimethyl ether (<b>7</b>), 5,3′,4′-trihydroxy-6,7-dimethoxy-flavone (<b>8</b>), and 2-methoxy-5-acetoxy-fruranogermacr-1(10)-en-6-one (<b>9</b>) as the major components. The computational study suggested that (<b>8</b>) and (<b>7</b>) were the most potent DPP-4 and α-Amylase inhibitors based on their lower binding affinities and extensive interactions with critical amino acid residues of the respective enzymes. The binding affinity of (<b>8</b>) with DPP-4 (−8.1 kcal/mol) was comparable to that of sitagliptin (−8.6 kcal/mol) while the binding affinity of (<b>7</b>) with α-Amylase (−8.6 kcal/mol) was better than acarbose (−6.9 kcal/mol). These findings highlight the phytochemical profile and potential antidiabetic compounds from <i>M. glabra</i> that may work as an alternative treatment for diabetes. |
| first_indexed | 2024-04-12T22:39:27Z |
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| language | English |
| last_indexed | 2024-04-12T22:39:27Z |
| publishDate | 2020-12-01 |
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| spelling | doaj.art-8001ddd4e0da4046aae9dbb7b604af5f2022-12-22T03:13:46ZengMDPI AGMolecules1420-30492020-12-01261110.3390/molecules26010001Identification of Dipeptidyl Peptidase-4 and α-Amylase Inhibitors from <i>Melicope glabra</i> (Blume) T. G. Hartley (Rutaceae) Using Liquid Chromatography Tandem Mass Spectrometry, In Vitro and In Silico MethodsAlexandra Quek0Nur Kartinee Kassim1Amin Ismail2Muhammad Alif Mohammad Latif3Khozirah Shaari4Dai Chuan Tan5Pei Cee Lim6Department of Chemistry, Faculty of Science, Universiti Putra Malaysia, Serdang, Selangor 43400, MalaysiaDepartment of Chemistry, Faculty of Science, Universiti Putra Malaysia, Serdang, Selangor 43400, MalaysiaDepartment of Nutrition and Dietetics, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, Serdang, Selangor 43400, MalaysiaDepartment of Chemistry, Faculty of Science, Universiti Putra Malaysia, Serdang, Selangor 43400, MalaysiaDepartment of Chemistry, Faculty of Science, Universiti Putra Malaysia, Serdang, Selangor 43400, MalaysiaDepartment of Chemistry, Faculty of Science, Universiti Putra Malaysia, Serdang, Selangor 43400, MalaysiaFaculty of Pharmacy, Mahsa University, Bandar Saujana Putra, Jenjarom, Selangor 42610, MalaysiaThe present study investigated the antidiabetic properties of the extracts and fractions from leaves and stem bark of <i>M. glabra</i> based on dipeptidyl peptidase-4 (DPP-4) and α-Amylase inhibitory activity assays. The chloroform extract of the leaves was found to be most active towards inhibition of DPP-4 and α-Amylase with IC<sub>50</sub> of 169.40 μg/mL and 303.64 μg/mL, respectively. Bioassay-guided fractionation of the leaves’ chloroform extract revealed fraction 4 (CF4) as the most active fraction (DPP-4 IC<sub>50</sub>: 128.35 μg/mL; α-Amylase IC<sub>50</sub>: 170.19 μg/mL). LC-MS/MS investigation of CF4 led to the identification of trans-decursidinol (<b>1</b>), swermirin (<b>2</b>), methyl 3,4,5-trimethoxycinnamate (<b>3</b>), renifolin (<b>4</b>), 4′,5,6,7-tetramethoxy-flavone (<b>5</b>), isorhamnetin (<b>6</b>), quercetagetin-3,4′-dimethyl ether (<b>7</b>), 5,3′,4′-trihydroxy-6,7-dimethoxy-flavone (<b>8</b>), and 2-methoxy-5-acetoxy-fruranogermacr-1(10)-en-6-one (<b>9</b>) as the major components. The computational study suggested that (<b>8</b>) and (<b>7</b>) were the most potent DPP-4 and α-Amylase inhibitors based on their lower binding affinities and extensive interactions with critical amino acid residues of the respective enzymes. The binding affinity of (<b>8</b>) with DPP-4 (−8.1 kcal/mol) was comparable to that of sitagliptin (−8.6 kcal/mol) while the binding affinity of (<b>7</b>) with α-Amylase (−8.6 kcal/mol) was better than acarbose (−6.9 kcal/mol). These findings highlight the phytochemical profile and potential antidiabetic compounds from <i>M. glabra</i> that may work as an alternative treatment for diabetes.https://www.mdpi.com/1420-3049/26/1/1<i>Melicope glabra</i>antidiabeticdiabetesDPP-4α-Amylasemolecular docking |
| spellingShingle | Alexandra Quek Nur Kartinee Kassim Amin Ismail Muhammad Alif Mohammad Latif Khozirah Shaari Dai Chuan Tan Pei Cee Lim Identification of Dipeptidyl Peptidase-4 and α-Amylase Inhibitors from <i>Melicope glabra</i> (Blume) T. G. Hartley (Rutaceae) Using Liquid Chromatography Tandem Mass Spectrometry, In Vitro and In Silico Methods Molecules <i>Melicope glabra</i> antidiabetic diabetes DPP-4 α-Amylase molecular docking |
| title | Identification of Dipeptidyl Peptidase-4 and α-Amylase Inhibitors from <i>Melicope glabra</i> (Blume) T. G. Hartley (Rutaceae) Using Liquid Chromatography Tandem Mass Spectrometry, In Vitro and In Silico Methods |
| title_full | Identification of Dipeptidyl Peptidase-4 and α-Amylase Inhibitors from <i>Melicope glabra</i> (Blume) T. G. Hartley (Rutaceae) Using Liquid Chromatography Tandem Mass Spectrometry, In Vitro and In Silico Methods |
| title_fullStr | Identification of Dipeptidyl Peptidase-4 and α-Amylase Inhibitors from <i>Melicope glabra</i> (Blume) T. G. Hartley (Rutaceae) Using Liquid Chromatography Tandem Mass Spectrometry, In Vitro and In Silico Methods |
| title_full_unstemmed | Identification of Dipeptidyl Peptidase-4 and α-Amylase Inhibitors from <i>Melicope glabra</i> (Blume) T. G. Hartley (Rutaceae) Using Liquid Chromatography Tandem Mass Spectrometry, In Vitro and In Silico Methods |
| title_short | Identification of Dipeptidyl Peptidase-4 and α-Amylase Inhibitors from <i>Melicope glabra</i> (Blume) T. G. Hartley (Rutaceae) Using Liquid Chromatography Tandem Mass Spectrometry, In Vitro and In Silico Methods |
| title_sort | identification of dipeptidyl peptidase 4 and α amylase inhibitors from i melicope glabra i blume t g hartley rutaceae using liquid chromatography tandem mass spectrometry in vitro and in silico methods |
| topic | <i>Melicope glabra</i> antidiabetic diabetes DPP-4 α-Amylase molecular docking |
| url | https://www.mdpi.com/1420-3049/26/1/1 |
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