ArticleCurrent research in food science2026
Identification of hTAS2R38 bitter taste receptor antagonists via homology modeling and molecular docking.
Article in Current research in food science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Taste Modulation by Umami Compounds: Mechanisms, Sensor-Based Evaluation, and Pharmaceutical Applications in Bitterness Suppression.Sensors (Basel, Switzerland) · 2026Review
- Elucidating the Material Basis and Receptor Mechanism of Bitterness inFoods (Basel, Switzerland) · 2026Article
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5 authors.
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Abstract
Taste receptor type 2 members (TAS2Rs), a family of G protein-coupled receptors, comprise a single polypeptide chain with seven transmembrane helices, three extracellular loops, and three intracellular loops. These receptors detect structurally diverse bitter compounds, playing a vital role in taste perception. Among them, TAS2R38 is a key bitter taste receptor that modulates bitter taste perception and dietary preferences. In this study, we focused on human TAS2R38, utilizing homology modeling based on squid rhodopsin (PDB ID: 3AYN) to predict its 3D structure. Potential antagonists were screened via molecular docking, with calcium imaging identifying Compound 58 as a promising candidate. Further docking analysis revealed that its amino group is critical for receptor binding. Our findings demonstrate that homology modeling combined with structure-based screening effectively identifies hTAS2R38 antagonists, offering insights for advancing bitterness-masking strategies.
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