---
title: "2,4-Thiazolidinedione Derivatives as Dual Inhibitors of α‑Amylase and α‑Glucosidase in Type 2 Diab"
id: "pubmed-42284877"
canonical_url: "https://medichelpline.com/clinical-feed/pubmed-42284877"
content_type: "clinical_feed_article"
specialty: "Pharmacology"
source_name: "PubMed / NCBI"
source_url: "https://pubmed.ncbi.nlm.nih.gov/42284877/"
doi: "10.1016/j.bioorg.2026.110083"
published_at: "2026-09-15T00:00:00.000Z"
evidence_level: "Journal Article"
license: "CC-BY-NC-4.0 / Informational Use"
---
# 2,4-Thiazolidinedione Derivatives as Dual Inhibitors of α‑Amylase and α‑Glucosidase in Type 2 Diab
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/pubmed-42284877
- **Specialty:** [Pharmacology](https://medichelpline.com/clinical-feed/pharmacology.md)
- **Primary Source:** PubMed / NCBI
- **Source URL:** [Original Journal Publication](https://pubmed.ncbi.nlm.nih.gov/42284877/)
- **DOI:** [10.1016/j.bioorg.2026.110083](https://doi.org/10.1016%2Fj.bioorg.2026.110083)
- **Published At:** 2026-09-15T00:00:00.000Z
- **Evidence Rating:** Journal Article
## Executive GIST (TL;DR)
- The study synthesized twenty-one **2,4-thiazolidinedione** (TZD) derivatives grouped as 5AT (a–g) and 5IT (a–n) and assessed them as dual inhibitors of carbohydrate‑digesting enzymes relevant to type 2 diabetes. - Molecular docking showed favorable binding affinities to **α‑glucosidase** (−7.1 to −9.7 kcal/mol) and **α‑amylase** (−8.5 to −10.7 kcal/mol), and ADME/drug‑likeness properties were reported as acceptable. - In vitro enzyme assays identified 5IT(b) as the most potent **α‑amylase** inhibitor (IC50 = 6.7 ± 0.2 μM), outperforming the reference drug **acarbose** (IC50 = 27.30 ± 0.1 μM). - Kinetic analysis for 5IT(b) indicated mixed‑type inhibition with Ki = 50.9 μM and Kis = 26.33 μM. - The methoxy‑substituted indole derivative 5IT(e) was the strongest **α‑glucosidase** inhibitor (IC50 = 10.89 ± 1.8 μM) and showed competitive inhibition with Ki = 18.8 μM. - Nine compounds (5IT[a], 5IT[b], 5IT[e], 5IT[f], 5IT[h], 5IT[i], 5IT[j], 5IT[l], 5IT[m]) demonstrated dual inhibitory activity against both enzymes in vitro. - The most active compounds exhibited favourable cell viability in MTT assays, supporting preliminary safety for further development. - Authors conclude that these TZD derivatives are promising leads for development of antidiabetic agents that target postprandial carbohydrate digestion via dual **α‑amylase** and **α‑glucosidase** inhibition.
## Clinical Analysis & Structured Key Points
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Epub 2026 Jun 9. # 2,4-thiazolidinediones as dual-target inhibitors against carbohydrate metabolism enzymes in type 2 diabetes [K Sruthi](https://pubmed.ncbi.nlm.nih.gov/?term=Sruthi+K&cauthor_id=42284877)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42284877/#full-view-affiliation-1 "Department of Chemistry, School of Advanced Sciences, Vellore Institute of Technology, Vellore 632014, India."), [Ayesha Noor](https://pubmed.ncbi.nlm.nih.gov/?term=Noor+A&cauthor_id=42284877)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42284877/#full-view-affiliation-2 "Center for Bio Separation Technology, Vellore Institute of Technology, Vellore 632014, India."), [Manju Sreedharannair L](https://pubmed.ncbi.nlm.nih.gov/?term=Sreedharannair+L+M&cauthor_id=42284877)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42284877/#full-view-affiliation-3 "Department of Chemistry, School of Advanced Sciences, Vellore Institute of Technology, Vellore 632014, India. Electronic address: slmanju@vit.ac.in.") Affiliations Expand ### Affiliations * 1 Department of Chemistry, School of Advanced Sciences, Vellore Institute of Technology, Vellore 632014, India. * 2 Center for Bio Separation Technology, Vellore Institute of Technology, Vellore 632014, India. * 3 Department of Chemistry, School of Advanced Sciences, Vellore Institute of Technology, Vellore 632014, India. Electronic address: slmanju@vit.ac.in. * PMID: **42284877** * DOI: [ 10.1016/j.bioorg.2026.110083 ](https://doi.org/10.1016/j.bioorg.2026.110083) Item in Clipboard # 2,4-thiazolidinediones as dual-target inhibitors against carbohydrate metabolism enzymes in type 2 diabetes K Sruthi et al. Bioorg Chem. 2026. Show details Display options Display options Format Abstract PubMed PMID Bioorg Chem Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Bioorg+Chem%22%5Bjour%5D&sort=date&sort_order=desc) * [ Search in NLM Catalog ](https://www.ncbi.nlm.nih.gov/nlmcatalog?term=%22Bioorg+Chem%22%5BTitle+Abbreviation%5D) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42284877/) . 2026 Sep 15:180:110083. doi: 10.1016/j.bioorg.2026.110083. Epub 2026 Jun 9. ### Authors [K Sruthi](https://pubmed.ncbi.nlm.nih.gov/?term=Sruthi+K&cauthor_id=42284877)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42284877/#short-view-affiliation-1 "Department of Chemistry, School of Advanced Sciences, Vellore Institute of Technology, Vellore 632014, India."), [Ayesha Noor](https://pubmed.ncbi.nlm.nih.gov/?term=Noor+A&cauthor_id=42284877)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42284877/#short-view-affiliation-2 "Center for Bio Separation Technology, Vellore Institute of Technology, Vellore 632014, India."), [Manju Sreedharannair L](https://pubmed.ncbi.nlm.nih.gov/?term=Sreedharannair+L+M&cauthor_id=42284877)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42284877/#short-view-affiliation-3 "Department of Chemistry, School of Advanced Sciences, Vellore Institute of Technology, Vellore 632014, India. Electronic address: slmanju@vit.ac.in.") ### Affiliations * 1 Department of Chemistry, School of Advanced Sciences, Vellore Institute of Technology, Vellore 632014, India. * 2 Center for Bio Separation Technology, Vellore Institute of Technology, Vellore 632014, India. * 3 Department of Chemistry, School of Advanced Sciences, Vellore Institute of Technology, Vellore 632014, India. Electronic address: slmanju@vit.ac.in. * PMID: **42284877** * DOI: [ 10.1016/j.bioorg.2026.110083 ](https://doi.org/10.1016/j.bioorg.2026.110083) Item in Clipboard Full text links Cite Display options Display options Format Abstract PubMed PMID ## Abstract The increasing prevalence of type 2 diabetes mellitus necessitates effective strategies targeting postprandial glucose dysregulation. Inhibition of α-amylase and α-glucosidase represents a validated therapeutic approach to limit carbohydrate digestion and glucose absorption. In this study, twenty-one 2,4-thiazolidinedione (TZD)-based derivatives, 5AT (a-g) and 5IT (a-n), were synthesised and evaluated using in silico and in vitro enzyme inhibition analyses. Molecular docking revealed strong binding affinities toward α-glucosidase (-7.1 to -9.7 kcal/mol) and α-amylase (-8.5 to -10.7 kcal/mol), supported by acceptable ADME and drug-likeness properties. Among the compounds, 5IT(b) displayed the most potent α-amylase inhibition (IC50 value = 6.7 ± 0.2 μM), surpassing the reference drug acarbose (IC50 = 27.30 ± 0.1 μM), and exhibited mixed-type inhibition with Ki and Kis values of 50.9 and 26.33 μM, respectively. The methoxy-substituted indole derivative 5IT(e) emerged as the strongest α-glucosidase inhibitor, with an IC50 of 10.89 ± 1.8 μM, and followed a competitive inhibition mechanism with a Ki value of 18.8 μM. Based on the in vitro assays, compounds 5IT(a), 5IT(b), 5IT(e), 5IT(f), 5IT(h), 5IT(i), 5IT(j), 5IT(l), and 5IT(m) demonstrated dual inhibitory activity since these compounds effectively inhibited both enzymes. Furthermore, the most potent compounds showed favourable cell viability. These results suggest that thiazolidinedione derivatives are promising dual α-amylase and α-glucosidase inhibitors for the development of antidiabetic therapies. **Keywords:** 2,4-thiazolidinedione; ADME; Kinetic analysis; MTT assay; Molecular docking; α-Glucosidase and α-amylase inhibition. Copyright © 2026 Elsevier Inc. All rights reserved. [PubMed Disclaimer](https://pubmed.ncbi.nlm.nih.gov/disclaimer/) ## Conflict of interest statement Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. ## Similar articles * [ Development of 1,2,3-Triazoles as Dual Enzyme Inhibitors Targeting α-Amylase and α-Glucosidase for Type 2 Diabetes Intervention. ](https://pubmed.ncbi.nlm.nih.gov/40899410/) Sruthi K, Manju SL.Sruthi K, et al.Arch Pharm (Weinheim). 2025 Sep;358(9):e70088. doi: 10.1002/ardp.70088.Arch Pharm (Weinheim). 2025.PMID: 40899410 * [ Synthesis and in vitro evaluation of chlorogenic acid amides as potential hypoglycemic agents and their synergistic effect with acarbose. ](https://pubmed.ncbi.nlm.nih.gov/34736132/) Cardullo N, Floresta G, Rescifina A, Muccilli V, Tringali C.Cardullo N, et al.Bioorg Chem. 2021 Dec;117:105458. doi: 10.1016/j.bioorg.2021.105458. Epub 2021 Oct 29.Bioorg Chem. 2021.PMID: 34736132 * [ Discovery of new anti-diabetic potential agents based on paracetamol incorporating sulfa-drugs: Design, synthesis, α-amylase, and α-glucosidase inhibitors with molecular docking simulation. ](https://pubmed.ncbi.nlm.nih.gov/38878516/) Khamees Thabet H, Ragab A, Imran M, Helal MH, Ibrahim Alaqel S, Alshehri A, Ash Mohd A, Rakan Alshammari M, S Abusaif M, A Ammar Y.Khamees Thabet H, et al.Eur J Med Chem. 2024 Sep 5;275:116589. doi: 10.1016/j.ejmech.2024.116589. Epub 2024 Jun 8.Eur J Med Chem. 2024.PMID: 38878516 * [ Unveiling anti-diabetic potential of new thiazole-sulfonamide derivatives: Design, synthesis, in vitro bio-evaluation targeting DPP-4, α-glucosidase, and α-amylase with in-silico ADMET and docking simulation. ](https://pubmed.ncbi.nlm.nih.gov/39067419/) Khamees Thabet H, Ammar YA, Imran M, Hamdy Helal M, Ibrahim Alaqel S, Alshehri A, Ash Mohd A, Abusaif MS, Ragab A.Khamees Thabet H, et al.Bioorg Chem. 2024 Oct;151:107671. doi: 10.1016/j.bioorg.2024.107671. Epub 2024 Jul 23.Bioorg Chem. 2024.PMID: 39067419 * [ ADME, Toxicity, Molecular Docking, Molecular Dynamics, Glucokinase activation, DPP-IV, α-amylase, and α-glucosidase Inhibition Assays of Mangiferin and Friedelin for Antidiabetic Potential. ](https://pubmed.ncbi.nlm.nih.gov/39714369/) Suryawanshi RM, Shimpi RB, Muralidharan V, Nemade LS, Gurugubelli S, Baig S, Vikhe SR, Dhawale SA, Mortuza MR, Sweilam SH, Siddiqui FA, Khan SL, Tutone M, Ahmad I, Begh MZA.Suryawanshi RM, et al.Chem Biodivers. 2025 May;22(5):e202402738. doi: 10.1002/cbdv.202402738. 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