Structure-Function Analyses of Human Bitter Taste Receptors—Where Do We Stand?

Behrens, Maik; Ziegler, Florian

doi:10.3390/molecules25194423

Cited by 23 publications

(11 citation statements)

References 122 publications

(167 reference statements)

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“…Bitter taste receptors are composed of a polypeptide chain that includes three intracellular and three extracellular loops and seven transmembrane helices [5]. The extracellular portion contains the most varied regions and the least conserved structure; it has an extracellular amino-terminal structural domain that binds strongly to bitter substances and plays a decisive role in bitter taste perception [6]. Bitter substances act on bitter taste receptor cells to produce excitatory effects, which are transmitted from the taste nerve to the nerve center, and enter the cerebral cortex to generate the perception of bitterness [7].…”

Section: Introductionmentioning

confidence: 99%

Molecular mechanisms of bitterness and astringency in the oral cavity induced by soyasaponin

Zhu,

Pan,

et al. 2024

Food Science and Human Wellness

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The interaction mechanism between soyasaponin (Ssa) and bitter receptors/mucin, as well as the saliva interface behavior of Ssa, were investigated to explore the presentation mechanism of Ssa bitterness and astringency (BA). Strong bitterness arising from high Ssa concentrations (0.5-1.5) mg/mL had a masking effect on astringency. At Ssa concentrations of (1-1.5) mg/mL, Ssa micelles altered the structure of mucin, exposing its internal tryptophan to a more polar environment. At Ssa concentrations of (0.05-1.5) mg/mL, its reaction with mucin increased the aggregation of particles in artificial saliva, which reduced the frictional lubricating properties of oral saliva. Ssa-mucin interactions affected the salivary interfacial adsorption layer, and their complexes synergistically reduced the interfacial tension. Ssa monomers and soyasapogenols bind to bitter receptors/mucin via hydrogen bonding and hydrophobic interactions. Class A Ssa binds more strongly than class B Ssa, and thus likely presents a higher BA. In conclusion, Ssa interacts with bitter receptors/mucin causing conformational changes and aggregation of salivary mucin, resulting in diminished frictional lubricating properties of oral saliva. This, in turn, affects taste perception and gustatory transmission.

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Section: Introductionmentioning

confidence: 99%

Molecular mechanisms of bitterness and astringency in the oral cavity induced by soyasaponin

Zhu,

Pan,

et al. 2024

Food Science and Human Wellness

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“…[ 4,5 ] hTAS2Rs are G protein‐coupled receptors (GPCRs) with seven transmembrane domains. [ 6 ] The binding between bitter substances and hTAS2Rs initiates signal transduction in taste cells, which results in bitterness perception. [ 7 ] Two strategies that can be considered for identifying bitterness and masking bitter taste: hTAS2R agonism and antagonism.…”

Section: Introductionmentioning

confidence: 99%

Bioelectronic Tongue for Identifying and Masking Bitterness Based on Bitter Taste Receptor Agonism and Antagonism

Hwang,

Kim,

Seo

et al. 2023

Adv Funct Materials

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Bitterness elicits unpleasant sensations in humans, which can hinder the acceptance of foods and medication adherence. Therefore, identifying and masking bitter tastes is crucial for developing palatable foods and promoting medication compliance in the food and pharmaceutical industries. To achieve this, employing agonism and antagonism of bitter taste receptors as effective strategies at the molecular level is essential. In this study, a bioelectronic tongue is developed to characterize the agonism and antagonism of bitter taste receptors. The human bitter taste receptors hTAS2R16 and hTAS2R31 are produced using an Escherichia coli expression system and reconstituted into nanodiscs (NDs). Subsequently, hTAS2R16‐ and hTAS2R31‐NDs are immobilized on the surface of graphene field‐effect transistors (FETs) to construct bioelectronic tongues. The developed system sensitively detected the bitter agonists, salicin and saccharin, at concentrations as low as 100 fM, with high selectivity in real‐time. The dose‐dependent curves shifted and K values decreased by the antagonists of hTAS2R16 and hTAS2R31, indicating antagonism‐based masking of bitter taste. Therefore, the developed bioelectronic tongue holds promise for identifying bitter tastes and evaluating the masking of bitterness based on the agonism and antagonism of hTAS2Rs.

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“…This is done by dimerizing different members into one receptor: the TAS1R1-TAS1R3 heterodimer is responsible for umami, while TAS1R2-TAS1R3 complex is responsible for sweet ( 7 ). On the other hand, the TAS2R family is made up of a much more diverse group of receptors, which in humans consists of 25 functional genes, as well as 8 pseudogenes, though the number varies greatly from species to species ( 8 , 9 ). Researchers have also discovered that although we possess a relatively low number of bitter taste receptors, we are able to detect as bitter thousands of compounds from a wide range of families.…”

Section: Introductionmentioning

confidence: 99%

The Hidden One: What We Know About Bitter Taste Receptor 39

et al. 2022

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Over thousands of years of evolution, animals have developed many ways to protect themselves. One of the most protective ways to avoid disease is to prevent the absorption of harmful components. This protective function is a basic role of bitter taste receptors (TAS2Rs), a G protein-coupled receptor family, whose presence in extraoral tissues has intrigued many researchers. In humans, there are 25 TAS2Rs, and although we know a great deal about some of them, others are still shrouded in mystery. One in this latter category is bitter taste receptor 39 (TAS2R39). Besides the oral cavity, it has also been found in the gastrointestinal tract and the respiratory, nervous and reproductive systems. TAS2R39 is a relatively non-selective receptor, which means that it can be activated by a range of mostly plant-derived compounds such as theaflavins, catechins and isoflavones. On the other hand, few antagonists for this receptor are available, since only some flavones have antagonistic properties (all of them detailed in the document). The primary role of TAS2R39 is to sense the bitter components of food and protect the organism from harmful compounds. There is also some indication that this bitter taste receptor regulates enterohormones and in turn, regulates food intake. In the respiratory system, it may be involved in the congestion process of allergic rhinitis and may stimulate inflammatory cytokines. However, more thorough research is needed to determine the precise role of TAS2R39 in these and other tissues.

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Structure-Function Analyses of Human Bitter Taste Receptors—Where Do We Stand?

Cited by 23 publications

References 122 publications

Molecular mechanisms of bitterness and astringency in the oral cavity induced by soyasaponin

Molecular mechanisms of bitterness and astringency in the oral cavity induced by soyasaponin

Bioelectronic Tongue for Identifying and Masking Bitterness Based on Bitter Taste Receptor Agonism and Antagonism

The Hidden One: What We Know About Bitter Taste Receptor 39

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