ArticleScientific reports2025
Synthesis and pharmacological profiling of cis-1-amino-2-indanol derivatives as α-glucosidase inhibitors.
Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
Indexed as
Identifiers
What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.