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.
Original language | English |
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Article number | 4623 |
Journal | Molecules |
Volume | 25 |
Issue number | 20 |
DOIs | |
State | Published - Oct 2020 |
Keywords
- Amino acids
- Docking
- GPCRs
- Homology modeling
- TAS2Rs