Evidence map›Paper›PMID 40378379›Full record

ArticlePloS one2025

Integrating in vitro and in silico approaches for exploring antidiabetic potential of dimethyl and thiomethyl indolinone derivatives.

Kashif Ali, Ahmed A Elhenawy, Waqas Alam, Khalaf F Alsharif, Khalid J Alzahrani, Haroon Khan, Long Chiau Ming, Rahul G Ingle

Abstract read
In one paragraph

Article in PloS one, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

8 authors.

Kashif AliDepartment of Pharmacy, Abdul Wali Khan University Mardan, Mardan, Pakistan.
Ahmed A ElhenawyChemistry Department, Faculty of Science, Al-Azhar University, Nasr City, Cairo, Egypt.
Waqas AlamDepartment of Pharmacy, Abdul Wali Khan University Mardan, Mardan, Pakistan.ORCID https://orcid.org/0000-0001-8329-9180
Khalaf F AlsharifDepartment of Clinical Laboratory Science, College of Applied Medical Science, Taif University, Taif, Saudi Arabia.
Khalid J AlzahraniDepartment of Clinical Laboratory Science, College of Applied Medical Science, Taif University, Taif, Saudi Arabia.ORCID https://orcid.org/0000-0002-6688-0106
Haroon KhanDepartment of Pharmacy, Abdul Wali Khan University Mardan, Mardan, Pakistan.ORCID https://orcid.org/0000-0002-1736-4404
Long Chiau MingFaculty of Medical and Life Sciences, Sunway University, Sunway City, Malaysia.ORCID https://orcid.org/0000-0002-6971-1383
Rahul G IngleDatta Meghe College of Pharmacy, Datta Meghe Institute of Higher Education and Research (Deemed to be University), Wardha, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Diabetes mellitus (DM) is a metabolic disorder caused by insulin deficiency. It is a rapidly growing problem with immense social, economic and health related problems. The market available drugs for the management of DM possess several limitations and therefore the discovery of more effective agents is the need of time. The current study was designed to evaluate two oxindole derivatives: (E)-3-(2,4-Dimethylbenzylidene)-6-chloroindolin-2-one (compound 1), and (E)-3-(4-(Methylthio) benzylidene)-6-chloroindolin-2-one (compound 2) against α-amylase, protein glycation, and DPP-IV. In case of in vitro antidiabetic activities, compound 1 demonstrated significant inhibition at various concentrations with IC50 value of 32.917 µg/mL against α-amylase, 210.592 µg/mL against protein glycation and 31.28 µg/mL against DPP-IV. Similarly, when tested at various concentrations, compound 2 illustrated marked inhibition with IC50 value of 42.691 µg/mL on α- amylase, 341.551 µg/mL on protein glycation and 47.192 µg/mL against DPP-IV. Molecular docking studies identified the binding patterns of oxindoles in the active site of targeted protein and enzymes. Moreover, the docking analysis also showed the potent interaction of test compounds with the target sites against α-amylase, protein glycation and DPP-IV. In conclusion, both the compounds are significant inhibitors of α-amylase, protein glycation and DPP-IV in vitro assays with the support of molecular dynamic studies and therefore are potential candidates for further studies.

Indexed as

Hypoglycemic AgentsIndolesalpha-AmylasesComputer SimulationDipeptidyl Peptidase 4GlycosylationHumansMolecular Docking SimulationOxindolesalpha-AmylasesDipeptidyl Peptidase 4Hypoglycemic AgentsIndolesOxindoles

Identifiers

PMID40378379
PMCPMC12084062

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Registered trials

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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 OpenQuestion graph.