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

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

  • Sci Rep. 2025 Dec 1;16(1):271. doi: 10.1038/s41598-025-29712-w.
Serab Khan 1 2,  Farzana Shaheen 2,  Liaqat Ali 3,  Ajmal Khan 4 5,  Muhammad U Anwar 1,  Atta Ullah 1,  Sobia Ahsan Halim 1,  Faizullah Khan 1,  Saeed Ullah 1,  Jalal Uddin 6,  Ahmed Al-Harrasi 1,  Javid Hussain 7
Affiliations

Affiliations

  • 1 Natural and Medical Sciences Research Centre, University of Nizwa, Nizwa, Sultanate of Oman.
  • 2 Third World Center for Science and Technology, H. E. J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi, 75270, Pakistan.
  • 3 Department of Chemistry, University of Mianwali, Mianwali, 42200, Pakistan.
  • 4 Natural and Medical Sciences Research Centre, University of Nizwa, Nizwa, Sultanate of Oman. [email protected].
  • 5 Department of Chemical and Biological Engineering, College of Engineering, Korea University, Seoul, 02841, Republic of Korea. [email protected].
  • 6 Department of Pharmaceutical Chemistry, College of Pharmacy, King Khalid University, 62529, Abha, Kingdom of Saudi Arabia.
  • 7 Department of Biological Sciences and Chemistry, College of Arts and Sciences, University of Nizwa, Nizwa, Sultanate of Oman.
PMID: 41326537 DOI: 10.1038/s41598-025-29712-w
Abstract

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.

Supplementary Information: The online version contains supplementary material available at 10.1038/s41598-025-29712-w.

Keywords

α-glucosidase; Aminoindanol; Docking; Iso(thio)cyanates; Kinetics.

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