期刊論文
| 學年 | 113 |
|---|---|
| 學期 | 1 |
| 出版（發表）日期 | 2025-01-28 |
| 作品名稱 | Exploring the inhibition of VEGFR2 tyrosine kinase domain by a novel Schiff base: Crystallographic and computational approaches towards anticancer potential |
| 作品名稱（其他語言） | |
| 著者 | Keerthan kumar; Sanjay Srivatsan; N. Maithra; B.S. Chethan; K Pruthviraj; S.V. Niranajna; Chih-Hsin Chen; K Sunil; N.K. Lokanath |
| 單位 | |
| 出版者 | |
| 著錄名稱、卷期、頁數 | Journal of Molecular Structure 1332, p.141552 |
| 摘要 | In this study, we developed a one-pot synthesis method to produce the Schiff base dimer derivative, 2-[4-(trifluoromethyl)benzyl]hydrazinecarbothioamide. This method involves the condensation of aldehyde and amine followed by sulfuric acid-catalysed dimerisation, yielding high-purity compounds with efficient reaction rates. The structural confirmation of the synthesised dimer was achieved through the spectroscopic technique such as FTIR, and single-crystal X-ray diffraction unveiled its dimeric framework formed through intermolecular hydrogen bonding interactions. Furthermore, computational studies such as density functional theory (DFT), quantum theory of atoms in molecules (QTAIM), molecular docking, and dynamic simulations were employed to elucidate the dimer's electronic structure and interaction properties. Notably, molecular docking analysis with the VEGFR2 receptor revealed potential biological interactions, indicating the compound's significant binding affinity and suggesting possible therapeutic applications. The integration of molecular dynamic simulations further confirmed the stability of the dimer-protein complexes, reinforcing the compound's potential efficacy in biological systems. |
| 關鍵字 | Synthesis; Crystal structure; DFT; Topology analysis; ADMET; Docking; Dynamic simulation |
| 語言 | en |
| ISSN | 0022-2860 |
| 期刊性質 | 國外 |
| 收錄於 | SCI |
| 產學合作 | |
| 通訊作者 | |
| 審稿制度 | 是 |
| 國別 | NLD |
| 公開徵稿 | |
| 出版型式 | ,電子版 |
| 相關連結 |
機構典藏連結 ( http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/127904 ) |