Evidence map›Paper›PMID 40576740›Full record

ArticleJournal of computer-aided molecular design2025

Design and evaluation of novel thiazolidinedione-oxadiazole derivatives as potent α-amylase inhibitors for antidiabetic therapy.

Pinky Arora, Aditi Rana, Azmat Ali Khan, Amer M Alanazi, Pankaj Wadhwa, Sonia Singla, Shubham Kumar, Rubal Kalra

Abstract read
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In one paragraph

Article in Journal of computer-aided molecular design, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Design, Synthesis,Molecules (Basel, Switzerland) · 2026
    Article
  2. 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.

Pinky AroraSchool of Bioengineering and Biosciences, Lovely Professional University, Jalandhar-Delhi G.T. Road, Phagwara, Punjab, 144411, India.
Aditi RanaG.H.G. KHalsa College of Pharmacy, Gurusar Sadhar, Ludhiana, Punjab, 141104, India.
Azmat Ali KhanPharmaceutical Biotechnology Laboratory, Department of Pharmaceutical Chemistry, College of Pharmacy, King Saud University, Riyadh, 11451, Saudi Arabia.
Amer M AlanaziPharmaceutical Biotechnology Laboratory, Department of Pharmaceutical Chemistry, College of Pharmacy, King Saud University, Riyadh, 11451, Saudi Arabia.
Pankaj WadhwaSchool of Pharmaceutical Sciences, Lovely Professional University, Jalandhar-Delhi G.T. Road, Phagwara, Punjab, 144411, India.
Sonia SinglaG.H.G. KHalsa College of Pharmacy, Gurusar Sadhar, Ludhiana, Punjab, 141104, India.
Shubham KumarSchool of Pharmaceutical Sciences, Lovely Professional University, Jalandhar-Delhi G.T. Road, Phagwara, Punjab, 144411, India. Shubhamm771@gmail.com.
Rubal KalraDepartment of Biomedical Engineering, 3120 Texas A&M University, 5045 Emerging Technologies Building, College Station, TX, 77843-3120, USA.

Funding

Ongoing Research Funding Program ORF-2025-339
6 · The paper itself

Abstract

Diabetes mellitus is a chronic metabolic disorder characterized by persistent hyperglycemia. Targeting α-amylase, a key enzyme involved in carbohydrate digestion, offers an effective strategy to manage postprandial glucose levels. In this study, a series of 31 novel thiazolidinedione-oxadiazole derivatives (SA1–SA31) were designed using pharmacophore-based strategies to incorporate diverse electron-withdrawing (EWGs) and electron-donating groups (EDGs). Molecular docking against α-amylase (PDB ID: 4W93) revealed superior binding affinities for compounds SA25 and SA31 (-10.3 and − 10.6 kcal/mol, respectively) compared to the standard drug Acarbose (-6.7 kcal/mol). Structure–activity relationship (SAR) analysis highlighted the significance of para-positioned EWGs in enhancing binding potential. ADME analysis of the top 15 compounds demonstrated favorable pharmacokinetic profiles with high gastrointestinal absorption and no Lipinski rule violations. Eight compounds were synthesized and characterized; their α-amylase inhibitory activities were evaluated. SA16 and SA19 showed potent inhibition with IC50 values of 9.15 µg/mL and 22.65 µg/mL, respectively. A Ramachandran plot analysis confirmed the structural validity of the target protein with 92.1% residues in favored regions. These findings underscore the potential of thiazolidinedione-oxadiazole hybrids as promising antidiabetic candidates and warrant further in vivo validation.

Indexed as

alpha-AmylasesEnzyme InhibitorsGlycoside Hydrolase InhibitorsHypoglycemic AgentsOxadiazolesThiazolidinedionesDrug DesignHumansMolecular Docking SimulationStructure-Activity Relationship2,4-thiazolidinedionealpha-AmylasesEnzyme InhibitorsGlycoside Hydrolase InhibitorsHypoglycemic AgentsOxadiazolesThiazolidinedionesADMETDiabetes mellitusIC50Molecular dockingOxadiazoleSARThiazolidinedioneα-amylase inhibition

Identifiers

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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.