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<p>Oxazole derived amide-based azomethines derivatives were synthesized through an efficient and facile route in this research work. By comparing with reference drug acarbose having IC<sub>50</sub> = 7.50 ± 0.20&#xa0;µM for α-amylase and 8.10 ± 0.40&#xa0;µM for <i>α</i>-glucosidase, it was revealed that all the novel synthesized analogues exhibit varying degree of inhibition against both enzymes. The remarkably good (top ranked) anti-diabetic competitor against both enzymes was found with IC<sub>50</sub> = 5.30 ± 0.20&#xa0;µM 5.80 ± 0.10&#xa0;µM) against <i>α</i>-amylase <i>α</i>-glucosidase, respectively. Other potent analogs of the series having IC<sub>50</sub> (6.90 ± 0.40, 7.20 ± 0.10&#xa0;µM), (7.60 ± 0.20, 8.10 ± 0.20&#xa0;µM) and (7.80 ± 0.20, 9.10 ± 0.10&#xa0;µM) also displayed excellent biological potential by engaging the active site of targeted enzymes through different interactions. The impact of substitutions on the drug profile of newly designed candidates was determined through the structure activity relationship. In silico molecular docking analysis was also conducted to predict that how the target proteins (enzyme) interact with the ligands by visualizing the 2D and 3D mode of binding interactions. The drug effectiveness of these analogues was assessed through ADMET analysis. By applying spectroscopic techniques <sup>1</sup>HNMR, <sup>13</sup>CNMR and HREI-MS the structural skeleton of newly designed analogues was identified. This study presents novel therapeutic agents for the future treatment of diabetes mellitus.</p> Graphical abstract <p></p>

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Novel oxazole derivatives as anti-diabetic agents along with in silico modeling: a critical analysis of recent trends and finding

  • 期刊论文

  • 发表日期：

    2025年9月26日

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  • Shoaib Khan,
  • Tayyiaba Iqbal,
  • Wajid Rehman,
  • Mujaddad Ur Rehman,
  • Rafaqat Hussain,
  • Aisha Bibi,
  • Ayed A. Dera

摘要

Oxazole derived amide-based azomethines derivatives were synthesized through an efficient and facile route in this research work. By comparing with reference drug acarbose having IC50 = 7.50 ± 0.20 µM for α-amylase and 8.10 ± 0.40 µM for α-glucosidase, it was revealed that all the novel synthesized analogues exhibit varying degree of inhibition against both enzymes. The remarkably good (top ranked) anti-diabetic competitor against both enzymes was found with IC50 = 5.30 ± 0.20 µM 5.80 ± 0.10 µM) against α-amylase α-glucosidase, respectively. Other potent analogs of the series having IC50 (6.90 ± 0.40, 7.20 ± 0.10 µM), (7.60 ± 0.20, 8.10 ± 0.20 µM) and (7.80 ± 0.20, 9.10 ± 0.10 µM) also displayed excellent biological potential by engaging the active site of targeted enzymes through different interactions. The impact of substitutions on the drug profile of newly designed candidates was determined through the structure activity relationship. In silico molecular docking analysis was also conducted to predict that how the target proteins (enzyme) interact with the ligands by visualizing the 2D and 3D mode of binding interactions. The drug effectiveness of these analogues was assessed through ADMET analysis. By applying spectroscopic techniques 1HNMR, 13CNMR and HREI-MS the structural skeleton of newly designed analogues was identified. This study presents novel therapeutic agents for the future treatment of diabetes mellitus.

Graphical abstract