Evidence map›Paper›PMID 41326537›Full record

ArticleScientific reports2025

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

Serab Khan, Farzana Shaheen, Liaqat Ali, Ajmal Khan, Muhammad U Anwar, Atta Ullah, Sobia Ahsan Halim, Faizullah Khan, Saeed Ullah, Jalal Uddin and 2 more

Abstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Serab KhanNatural and Medical Sciences Research Centre, University of Nizwa, Nizwa, Sultanate of Oman.
Farzana ShaheenThird 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.
Liaqat AliDepartment of Chemistry, University of Mianwali, Mianwali, 42200, Pakistan.
Ajmal KhanNatural and Medical Sciences Research Centre, University of Nizwa, Nizwa, Sultanate of Oman. ajmalkhan@unizwa.edu.om.
Muhammad U AnwarNatural and Medical Sciences Research Centre, University of Nizwa, Nizwa, Sultanate of Oman.
Atta UllahNatural and Medical Sciences Research Centre, University of Nizwa, Nizwa, Sultanate of Oman.
Sobia Ahsan HalimNatural and Medical Sciences Research Centre, University of Nizwa, Nizwa, Sultanate of Oman.
Faizullah KhanNatural and Medical Sciences Research Centre, University of Nizwa, Nizwa, Sultanate of Oman.
Saeed UllahNatural and Medical Sciences Research Centre, University of Nizwa, Nizwa, Sultanate of Oman.
Jalal UddinDepartment of Pharmaceutical Chemistry, College of Pharmacy, King Khalid University, 62529, Abha, Kingdom of Saudi Arabia.
Ahmed Al-HarrasiNatural and Medical Sciences Research Centre, University of Nizwa, Nizwa, Sultanate of Oman. aharrasi@unizwa.edu.om.
Javid HussainDepartment of Biological Sciences and Chemistry, College of Arts and Sciences, University of Nizwa, Nizwa, Sultanate of Oman. javidhej@unizwa.edu.om.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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

alpha-GlucosidasesGlycoside Hydrolase InhibitorsIndansCatalytic DomainKineticsMolecular Docking SimulationStructure-Activity Relationshipalpha-GlucosidasesGlycoside Hydrolase InhibitorsIndansAminoindanolDockingIso(thio)cyanatesKineticsα-glucosidase

Identifiers

PMID41326537
PMCPMC12770330

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.