Design, Synthesis, enzyme inhibitory activity and molecular docking studies of new 1,2,3-triazole linked nucleobases
Thirteen novel 1,2,3-triazole linked nucleobases (5a-m) were designed and efficiently synthesized as potential human enzyme inhibitors. The target compounds were synthesized by using Copper (I)-catalysed Huisgen-Sharpless-Meldal 1,3-dipolar cycloaddition reaction of propargylated nucleobases and sub...
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| Language: | English |
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Elsevier
2025-01-01
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| Series: | Results in Chemistry |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211715624007070 |
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| author | Aditya Aggarwal Chanchal Vashisth Komal Bharti Neera Raghav Surender Kumar |
| author_facet | Aditya Aggarwal Chanchal Vashisth Komal Bharti Neera Raghav Surender Kumar |
| author_sort | Aditya Aggarwal |
| collection | DOAJ |
| description | Thirteen novel 1,2,3-triazole linked nucleobases (5a-m) were designed and efficiently synthesized as potential human enzyme inhibitors. The target compounds were synthesized by using Copper (I)-catalysed Huisgen-Sharpless-Meldal 1,3-dipolar cycloaddition reaction of propargylated nucleobases and substituted aryl azides in good yield. Compounds (5a-m) were characterized by their 1HNMR, 13C NMR, 2D NMR and mass spectral data. All compounds were screened in vitro for their inhibitory efficacy against pepsin, trypsin, lipase and α-amylase enzymes. All the compounds showed more than 50 % inhibition against these enzymes. Interestingly, four compounds, including 5d, 5h, 5k and 5m displayed excellent potent level of enzyme inhibitory activity at 10−7 M concentration. Further, molecular docking analysis revealed that some compounds shown significant binding interactions with target sites. Compound 5h exhibited the highest enzyme inhibitory activity (trypsin, % inhibition = 81.55) at 10−7 M concentration in comparison to the reference drug orlistat. |
| format | Article |
| id | doaj-art-47ded542b64641bc9ea06d1ee0fef930 |
| institution | Kabale University |
| issn | 2211-7156 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Results in Chemistry |
| spelling | doaj-art-47ded542b64641bc9ea06d1ee0fef9302025-01-29T05:00:55ZengElsevierResults in Chemistry2211-71562025-01-0113102011Design, Synthesis, enzyme inhibitory activity and molecular docking studies of new 1,2,3-triazole linked nucleobasesAditya Aggarwal0Chanchal Vashisth1Komal Bharti2Neera Raghav3Surender Kumar4Bioorganic Laboratory, Department of Chemistry, Institute of Integrated and Honors Studies (IIHS), Kurukshetra University, Kurukshetra, Haryana 136119, IndiaDepartment of Chemistry, Kurukshetra University, Kurukshetra, Haryana 136119, IndiaBioorganic Laboratory, Department of Chemistry, Institute of Integrated and Honors Studies (IIHS), Kurukshetra University, Kurukshetra, Haryana 136119, IndiaDepartment of Chemistry, Kurukshetra University, Kurukshetra, Haryana 136119, IndiaBioorganic Laboratory, Department of Chemistry, Institute of Integrated and Honors Studies (IIHS), Kurukshetra University, Kurukshetra, Haryana 136119, India; Corresponding author.Thirteen novel 1,2,3-triazole linked nucleobases (5a-m) were designed and efficiently synthesized as potential human enzyme inhibitors. The target compounds were synthesized by using Copper (I)-catalysed Huisgen-Sharpless-Meldal 1,3-dipolar cycloaddition reaction of propargylated nucleobases and substituted aryl azides in good yield. Compounds (5a-m) were characterized by their 1HNMR, 13C NMR, 2D NMR and mass spectral data. All compounds were screened in vitro for their inhibitory efficacy against pepsin, trypsin, lipase and α-amylase enzymes. All the compounds showed more than 50 % inhibition against these enzymes. Interestingly, four compounds, including 5d, 5h, 5k and 5m displayed excellent potent level of enzyme inhibitory activity at 10−7 M concentration. Further, molecular docking analysis revealed that some compounds shown significant binding interactions with target sites. Compound 5h exhibited the highest enzyme inhibitory activity (trypsin, % inhibition = 81.55) at 10−7 M concentration in comparison to the reference drug orlistat.http://www.sciencedirect.com/science/article/pii/S2211715624007070123-Triazole3-Dipolar cycloadditionNucleobasesEnzyme inhibitor |
| spellingShingle | Aditya Aggarwal Chanchal Vashisth Komal Bharti Neera Raghav Surender Kumar Design, Synthesis, enzyme inhibitory activity and molecular docking studies of new 1,2,3-triazole linked nucleobases Results in Chemistry 1 2 3-Triazole 3-Dipolar cycloaddition Nucleobases Enzyme inhibitor |
| title | Design, Synthesis, enzyme inhibitory activity and molecular docking studies of new 1,2,3-triazole linked nucleobases |
| title_full | Design, Synthesis, enzyme inhibitory activity and molecular docking studies of new 1,2,3-triazole linked nucleobases |
| title_fullStr | Design, Synthesis, enzyme inhibitory activity and molecular docking studies of new 1,2,3-triazole linked nucleobases |
| title_full_unstemmed | Design, Synthesis, enzyme inhibitory activity and molecular docking studies of new 1,2,3-triazole linked nucleobases |
| title_short | Design, Synthesis, enzyme inhibitory activity and molecular docking studies of new 1,2,3-triazole linked nucleobases |
| title_sort | design synthesis enzyme inhibitory activity and molecular docking studies of new 1 2 3 triazole linked nucleobases |
| topic | 1 2 3-Triazole 3-Dipolar cycloaddition Nucleobases Enzyme inhibitor |
| url | http://www.sciencedirect.com/science/article/pii/S2211715624007070 |
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