ArticlePloS one2019
Triazoloquinazolines as a new class of potent α-glucosidase inhibitors: in vitro evaluation and docking study.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Identification of α-glucosidase inhibitory phytochemicals from Erythrina crista-galli using combined experimental and computational methods.BMC chemistry · 2026Article
- Synthesis, in vitro, and in silico studies of 4-chlorophenyl-sulfonyl Indole based thiosemicarbazones as competitive α-glucosidase inhibitors.Scientific reports · 2025Article
- Quinazolines [Molecules (Basel, Switzerland) · 2025Review
- Click Reaction Inspired Enzyme Inhibitors in Diabetes Care: An Update in the Field of Chronic Metabolic Disorder.Current pharmaceutical design · 2025Review
- Construction of an MLR-QSAR Model Based on Dietary Flavonoids and Screening of Natural α-Glucosidase Inhibitors.Foods (Basel, Switzerland) · 2022Article
- Molecular Structure-Based Screening of the Constituents ofCurrent issues in molecular biology · 2022Article
- Synthesis and Evaluation of Coumarin-Chalcone Derivatives as α-Glucosidase Inhibitors.Frontiers in chemistry · 2022Article
- A review of alpha-glucosidase inhibitors from plants as potential candidates for the treatment of type-2 diabetes.Phytochemistry reviews : proceedings of the Phytochemical Society of Europe · 2022Review
- In Silico Approaches to Identify Polyphenol Compounds as α-Glucosidase and α-Amylase Inhibitors against Type-II Diabetes.Biomolecules · 2021Review
- Article
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6 authors.
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Abstract
Previously, we synthesized triazoloquinazolines 1-14 and characterized their structure. In this study, we aimed to evaluate the in vitro activity of the targets 1-14 as α-glucosidase inhibitors using α-glucosidase enzyme from Saccharomyces cerevisiae type 1. Among the tested compounds, triazoloquinazolines 14, 8, 4, 5, and 3 showed the highest inhibitory activity (IC50 = 12.70 ± 1.87, 28.54 ± 1.22, 45.65 ± 4.28, 72.28 ± 4.67, and 83.87 ± 5.12 μM, respectively) in relation to that of acarbose (IC50 = 143.54 ± 2.08 μM) as a reference drug. Triazoloquinazolines were identified herein as a new class of potent α-glucosidase inhibitors. Molecular docking results envisaged the plausible binding interaction between the target triazoloquinazolines and α-glucosidase enzyme and indicated considerable interaction with the active site residues.
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