Scholarlink

<p>By treating <i>cis</i>-1-amino-2-indanol with different functionalized isocyanates and isothiocyanates, a group of 15 indanol derivatives were synthesized. The synthesis was effectively performed employing a previously proven method and the resulting products were characterized through multiple spectroscopic techniques including NMR spectroscopy and the <i>α</i>-glucosidase inhibitory assay was used to evaluate their α-glucosidase inhibitory capacity. The results indicated a varied level of inhibitory activity against <i>α</i>-glucosidase and <b>2h</b> showed the highest potency with IC<sub>50</sub> value of 9.64 ± 0.24 µM, while compounds <b>2g</b>, <b>2c</b>, and <b>3i</b> also exhibited significant inhibition. The kinetic analysis of the most active inhibitor <b>2h</b> showed its competitive mode of inhibition, with a <i>Ki</i> value of 7.39 ± 0.088 µM. The binding modes of compounds were predicted by molecular docking analysis within the active site of <i>α</i>-glucosidase enzyme, where our molecules showed significant binding and docking scores. Docking analysis revealed that the thiourea and urea moieties play a critical role in facilitating the interaction of the molecules with one of the catalytic triad residues. The current study provides a basis for the development of a possible lead compound that can inhibit α-glucosidase.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Synthesis and pharmacological profiling of cis-1-amino-2-indanol derivatives as α-glucosidase inhibitors

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2025年12月1日

查看全文
  • Serab Khan,
  • Farzana Shaheen,
  • Liaqat Ali,
  • Ajmal Khan,
  • Muhammad U. Anwar,
  • Atta Ullah,
  • Sobia Ahsan Halim,
  • Faizullah Khan,
  • Saeed Ullah,
  • Jalal Uddin,
  • Ahmed Al-Harrasi,
  • Javid Hussain

摘要

By treating cis-1-amino-2-indanol with different functionalized isocyanates and isothiocyanates, a group of 15 indanol derivatives were synthesized. The synthesis was effectively performed employing a previously proven method and the resulting products were characterized through multiple spectroscopic techniques including NMR spectroscopy and the α-glucosidase inhibitory assay was used to evaluate their α-glucosidase inhibitory capacity. The results indicated a varied level of inhibitory activity against α-glucosidase and 2h showed the highest potency with IC50 value of 9.64 ± 0.24 µM, while compounds 2g, 2c, and 3i also exhibited significant inhibition. The kinetic analysis of the most active inhibitor 2h showed its competitive mode of inhibition, with a Ki value of 7.39 ± 0.088 µM. The binding modes of compounds were predicted by molecular docking analysis within the active site of α-glucosidase enzyme, where our molecules showed significant binding and docking scores. Docking analysis revealed that the thiourea and urea moieties play a critical role in facilitating the interaction of the molecules with one of the catalytic triad residues. The current study provides a basis for the development of a possible lead compound that can inhibit α-glucosidase.