Experimental and Computational Analysis of Newly Synthesized Benzotriazinone Sulfonamides as Alpha-Glucosidase Inhibitors.
- Publisher:
- MDPI
- Publication Type:
- Journal Article
- Citation:
- Molecules, 2022, 27, (20), pp. 6783
- Issue Date:
- 2022-10-11
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Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Khalid, Z | |
dc.contributor.author | Alnuwaiser, MA | |
dc.contributor.author | Ahmad, HA | |
dc.contributor.author | Shafqat, SS | |
dc.contributor.author | Munawar, MA | |
dc.contributor.author | Kamran, K | |
dc.contributor.author | Abbas, MM | |
dc.contributor.author | Kalam, MA | |
dc.contributor.author | Ewida, MA | |
dc.date.accessioned | 2023-01-31T02:07:31Z | |
dc.date.available | 2022-09-21 | |
dc.date.available | 2023-01-31T02:07:31Z | |
dc.date.issued | 2022-10-11 | |
dc.identifier.citation | Molecules, 2022, 27, (20), pp. 6783 | |
dc.identifier.issn | 1420-3049 | |
dc.identifier.issn | 1420-3049 | |
dc.identifier.uri | http://hdl.handle.net/10453/165644 | |
dc.description.abstract | Diabetes mellitus is a chronic metabolic disorder in which the pancreas secretes insulin but the body cells do not recognize it. As a result, carbohydrate metabolism causes hyperglycemia, which may be fatal for various organs. This disease is increasing day by day and it is prevalent among people of all ages, including young adults and children. Acarbose and miglitol are famous alpha-glucosidase inhibitors but they complicate patients with the problems of flatulence, pain, bloating, diarrhea, and loss of appetite. To overcome these challenges, it is crucial to discover new anti-diabetic drugs with minimal side effects. For this purpose, benzotriazinone sulfonamides were synthesized and their structures were characterized by FT-IR, 1H-NMR and 13C-NMR spectroscopy. In vitro alpha-glucosidase inhibition studies of all synthesized hybrids were conducted using the spectrophotometric method. The synthesized compounds revealed moderate-to-good inhibition activity; in particular, nitro derivatives 12e and 12f were found to be the most effective inhibitors against this enzyme, with IC50 values of 32.37 ± 0.15 µM and 37.75 ± 0.11 µM. In silico studies, including molecular docking as well as DFT analysis, also strengthened the experimental findings. Both leading compounds 12e and 12f showed strong hydrogen bonding interactions within the enzyme cavity. DFT studies also reinforced the strong binding interactions of these derivatives with biological molecules due to their lowest chemical hardness values and lowest orbital energy gap values. | |
dc.format | Electronic | |
dc.language | eng | |
dc.publisher | MDPI | |
dc.relation.ispartof | Molecules | |
dc.relation.isbasedon | 10.3390/molecules27206783 | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | 0304 Medicinal and Biomolecular Chemistry, 0305 Organic Chemistry, 0307 Theoretical and Computational Chemistry | |
dc.subject.classification | Organic Chemistry | |
dc.subject.mesh | Child | |
dc.subject.mesh | Humans | |
dc.subject.mesh | Glycoside Hydrolase Inhibitors | |
dc.subject.mesh | alpha-Glucosidases | |
dc.subject.mesh | Molecular Docking Simulation | |
dc.subject.mesh | Acarbose | |
dc.subject.mesh | Sulfonamides | |
dc.subject.mesh | Spectroscopy, Fourier Transform Infrared | |
dc.subject.mesh | Structure-Activity Relationship | |
dc.subject.mesh | Diabetes Mellitus | |
dc.subject.mesh | Sulfanilamide | |
dc.subject.mesh | Insulins | |
dc.subject.mesh | Molecular Structure | |
dc.subject.mesh | Humans | |
dc.subject.mesh | Diabetes Mellitus | |
dc.subject.mesh | Sulfonamides | |
dc.subject.mesh | alpha-Glucosidases | |
dc.subject.mesh | Acarbose | |
dc.subject.mesh | Spectroscopy, Fourier Transform Infrared | |
dc.subject.mesh | Molecular Structure | |
dc.subject.mesh | Structure-Activity Relationship | |
dc.subject.mesh | Child | |
dc.subject.mesh | Insulins | |
dc.subject.mesh | Molecular Docking Simulation | |
dc.subject.mesh | Glycoside Hydrolase Inhibitors | |
dc.subject.mesh | Sulfanilamide | |
dc.title | Experimental and Computational Analysis of Newly Synthesized Benzotriazinone Sulfonamides as Alpha-Glucosidase Inhibitors. | |
dc.type | Journal Article | |
utslib.citation.volume | 27 | |
utslib.location.activity | Switzerland | |
utslib.for | 0304 Medicinal and Biomolecular Chemistry | |
utslib.for | 0305 Organic Chemistry | |
utslib.for | 0307 Theoretical and Computational Chemistry | |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Engineering and Information Technology | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Engineering and Information Technology/School of Civil and Environmental Engineering | |
utslib.copyright.status | open_access | * |
dc.date.updated | 2023-01-31T02:06:38Z | |
pubs.issue | 20 | |
pubs.publication-status | Published online | |
pubs.volume | 27 | |
utslib.citation.issue | 20 |
Abstract:
Diabetes mellitus is a chronic metabolic disorder in which the pancreas secretes insulin but the body cells do not recognize it. As a result, carbohydrate metabolism causes hyperglycemia, which may be fatal for various organs. This disease is increasing day by day and it is prevalent among people of all ages, including young adults and children. Acarbose and miglitol are famous alpha-glucosidase inhibitors but they complicate patients with the problems of flatulence, pain, bloating, diarrhea, and loss of appetite. To overcome these challenges, it is crucial to discover new anti-diabetic drugs with minimal side effects. For this purpose, benzotriazinone sulfonamides were synthesized and their structures were characterized by FT-IR, 1H-NMR and 13C-NMR spectroscopy. In vitro alpha-glucosidase inhibition studies of all synthesized hybrids were conducted using the spectrophotometric method. The synthesized compounds revealed moderate-to-good inhibition activity; in particular, nitro derivatives 12e and 12f were found to be the most effective inhibitors against this enzyme, with IC50 values of 32.37 ± 0.15 µM and 37.75 ± 0.11 µM. In silico studies, including molecular docking as well as DFT analysis, also strengthened the experimental findings. Both leading compounds 12e and 12f showed strong hydrogen bonding interactions within the enzyme cavity. DFT studies also reinforced the strong binding interactions of these derivatives with biological molecules due to their lowest chemical hardness values and lowest orbital energy gap values.
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