Insights from in silico exploration of major curcumin analogs targeting human dipeptidyl peptidase IV
The goal of this work is to use a variety of in-silico techniques to identify anti-diabetic agents against DPP-IV enzyme from five main curcumin analogues. To produce the successful molecules, five main curcumin analogues were docked into the active site of DPP-IV enzyme. In comparison to the contro...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English English |
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Taylor & Francis
2024
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| Online Access: | http://umpir.ump.edu.my/id/eprint/41689/1/Insights%20from%20in%20silico%20exploration%20of%20major%20curcumin%20analogs%20targeting%20human%20dipeptidyl.pdf http://umpir.ump.edu.my/id/eprint/41689/2/Insights%20from%20in%20silico%20exploration%20of%20major%20curcumin%20analogs%20targeting%20human%20dipeptidyl%20peptidase%20IV.pdf |
| _version_ | 1825815736924241920 |
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| author | Roney, Miah Dubey, Amit Issahaku, Abdul Rashid Uddin, Md. Nazim Tufail, Aisha Wilhelm, Anke Normaiza, Zamri Mohd Fadhlizil Fasihi, Mohd Aluwi |
| author_facet | Roney, Miah Dubey, Amit Issahaku, Abdul Rashid Uddin, Md. Nazim Tufail, Aisha Wilhelm, Anke Normaiza, Zamri Mohd Fadhlizil Fasihi, Mohd Aluwi |
| author_sort | Roney, Miah |
| collection | UMP |
| description | The goal of this work is to use a variety of in-silico techniques to identify anti-diabetic agents against DPP-IV enzyme from five main curcumin analogues. To produce the successful molecules, five main curcumin analogues were docked into the active site of DPP-IV enzyme. In comparison to the control molecule (Saxagliptin, −6.9 kcal/mol), all the compounds have the highest binding affinity (-7.6 to −7.7 kcal/mol) for the DPP-IV enzyme. These compounds underwent further testing for studies on drug-likeness, pharmacokinetics, and acute toxicity to see the efficacy and safety of compounds. To assess the stability of the docking complex and the binding posture identified during the docking experiment, our study got THC as the lead compound, which was then exposed to 200 ns of molecular dynamic simulation and PCA analysis. Additionally, DFT calculations were conducted to determine the thermodynamic, molecular orbital, and electrostatic potential characteristics of lead compound. Overall, the lead chemical has shown strong drug-like properties, is non-toxic, and has a sizable affinity for the DPP-IV enzyme. |
| first_indexed | 2024-09-25T03:50:44Z |
| format | Article |
| id | UMPir41689 |
| institution | Universiti Malaysia Pahang |
| language | English English |
| last_indexed | 2024-09-25T03:50:44Z |
| publishDate | 2024 |
| publisher | Taylor & Francis |
| record_format | dspace |
| spelling | UMPir416892024-06-26T04:13:58Z http://umpir.ump.edu.my/id/eprint/41689/ Insights from in silico exploration of major curcumin analogs targeting human dipeptidyl peptidase IV Roney, Miah Dubey, Amit Issahaku, Abdul Rashid Uddin, Md. Nazim Tufail, Aisha Wilhelm, Anke Normaiza, Zamri Mohd Fadhlizil Fasihi, Mohd Aluwi HD Industries. Land use. Labor TP Chemical technology The goal of this work is to use a variety of in-silico techniques to identify anti-diabetic agents against DPP-IV enzyme from five main curcumin analogues. To produce the successful molecules, five main curcumin analogues were docked into the active site of DPP-IV enzyme. In comparison to the control molecule (Saxagliptin, −6.9 kcal/mol), all the compounds have the highest binding affinity (-7.6 to −7.7 kcal/mol) for the DPP-IV enzyme. These compounds underwent further testing for studies on drug-likeness, pharmacokinetics, and acute toxicity to see the efficacy and safety of compounds. To assess the stability of the docking complex and the binding posture identified during the docking experiment, our study got THC as the lead compound, which was then exposed to 200 ns of molecular dynamic simulation and PCA analysis. Additionally, DFT calculations were conducted to determine the thermodynamic, molecular orbital, and electrostatic potential characteristics of lead compound. Overall, the lead chemical has shown strong drug-like properties, is non-toxic, and has a sizable affinity for the DPP-IV enzyme. Taylor & Francis 2024 Article PeerReviewed pdf en http://umpir.ump.edu.my/id/eprint/41689/1/Insights%20from%20in%20silico%20exploration%20of%20major%20curcumin%20analogs%20targeting%20human%20dipeptidyl.pdf pdf en http://umpir.ump.edu.my/id/eprint/41689/2/Insights%20from%20in%20silico%20exploration%20of%20major%20curcumin%20analogs%20targeting%20human%20dipeptidyl%20peptidase%20IV.pdf Roney, Miah and Dubey, Amit and Issahaku, Abdul Rashid and Uddin, Md. Nazim and Tufail, Aisha and Wilhelm, Anke and Normaiza, Zamri and Mohd Fadhlizil Fasihi, Mohd Aluwi (2024) Insights from in silico exploration of major curcumin analogs targeting human dipeptidyl peptidase IV. Journal of Biomolecular Structure and Dynamics. pp. 1-15. ISSN 0739-1102. (In Press / Online First) (In Press / Online First) https://doi.org/10.1080/07391102.2024.2306197 10.1080/07391102.2024.2306197 |
| spellingShingle | HD Industries. Land use. Labor TP Chemical technology Roney, Miah Dubey, Amit Issahaku, Abdul Rashid Uddin, Md. Nazim Tufail, Aisha Wilhelm, Anke Normaiza, Zamri Mohd Fadhlizil Fasihi, Mohd Aluwi Insights from in silico exploration of major curcumin analogs targeting human dipeptidyl peptidase IV |
| title | Insights from in silico exploration of major curcumin analogs targeting human dipeptidyl peptidase IV |
| title_full | Insights from in silico exploration of major curcumin analogs targeting human dipeptidyl peptidase IV |
| title_fullStr | Insights from in silico exploration of major curcumin analogs targeting human dipeptidyl peptidase IV |
| title_full_unstemmed | Insights from in silico exploration of major curcumin analogs targeting human dipeptidyl peptidase IV |
| title_short | Insights from in silico exploration of major curcumin analogs targeting human dipeptidyl peptidase IV |
| title_sort | insights from in silico exploration of major curcumin analogs targeting human dipeptidyl peptidase iv |
| topic | HD Industries. Land use. Labor TP Chemical technology |
| url | http://umpir.ump.edu.my/id/eprint/41689/1/Insights%20from%20in%20silico%20exploration%20of%20major%20curcumin%20analogs%20targeting%20human%20dipeptidyl.pdf http://umpir.ump.edu.my/id/eprint/41689/2/Insights%20from%20in%20silico%20exploration%20of%20major%20curcumin%20analogs%20targeting%20human%20dipeptidyl%20peptidase%20IV.pdf |
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