ArticleMolecules (Basel, Switzerland)2020
In Silico Molecular Study of Tryptophan Bitterness.
Article in Molecules (Basel, Switzerland), 2020. 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, 23 citations in OpenAlex.
- Sex-Specific Differences in Quality and Flavor Traits of Gonads from the Sea Urchin (Foods (Basel, Switzerland) · 2026Article
- De novo design and experimental characterization of bitter peptides.NPJ science of food · 2026Article
- Comprehensive Taste Profile Assessment of Underexplored Amino Acids and Protein Derivatives in Umami and Koku.Foods (Basel, Switzerland) · 2026Article
- Multi-dimensional information characterization of different grades ofFrontiers in nutrition · 2026Article
- Tryptophan Stability and Palatability in the Food Formulation: A Review.Current pharmaceutical biotechnology · 2025Review
- Bitter peptide prediction using graph neural networks.Journal of cheminformatics · 2024Article
- Combined full-length transcriptomic and metabolomic analysis reveals the molecular mechanisms underlying nutrients and taste components development in Primulina juliae.BMC genomic data · 2024Article
- Membrane-bound chemoreception of bitter bile acids and peptides is mediated by the same subset of bitter taste receptors.Cellular and molecular life sciences : CMLS · 2024Article
- Modeling the Orthosteric Binding Site of the G Protein-Coupled Odorant Receptor OR5K1.Journal of chemical information and modeling · 2023Article
- Bioactive and Sensory Di- and Tripeptides Generated during Dry-Curing of Pork Meat.International journal of molecular sciences · 2023Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tryptophan is an essential amino acid, required for the production of serotonin. It is the most bitter amino acid and its bitterness was found to be mediated by the bitter taste receptor TAS2R4. Di-tryptophan has a different selectivity profile and was found to activate three bitter taste receptors, whereas tri-tryptophan activated five TAS2Rs. In this work, the selectivity/promiscuity profiles of the mono-to-tri-tryptophans were explored using molecular modeling simulations to provide new insights into the molecular recognition of the bitter tryptophan. Tryptophan epitopes were found in all five peptide-sensitive TAS2Rs and the best tryptophan epitope was identified and characterized at the core of the orthosteric binding site of TAS2R4.
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Registered trials
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