Identification and molecular docking of peptides from <i>Mizuhopecten yessoensis</i> myosin as human bitter taste receptor T2R14 blockers

Zhao, Wenzhu; Li, Donghui; Wang, Yingxue; Kan, Ruotong; Ji, Huizhuo; Su, Lijun; Yu, Zhipeng; Lǐ, Jiànróng

doi:10.1039/d1fo02447g

Cited by 11 publications

(5 citation statements)

References 29 publications

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“…In a study by Lin et al, 18 it was found that N-acetyl-valine/Leu/Ile/Met/Phe were kokumi complexes that could enhance sweetness, umami, and saltiness. Zhao et al 28 identified potential bitter taste receptor T2R14 blockers from the myosin of Mizuhopecten yessoensis and verified the in vitro T2R14 blocking activity of the selected peptides by electronic tongue. The results showed that QRPR had T2R14 blocking activity with an IC 50 value of 256.69 ± 1.91 μM.…”

Section: Nmr Characterization Of Lpmentioning

confidence: 98%

A Novel Compound with Kokumi Properties: Enzymatic Preparation and Taste Presentation Evaluation of N-Lauroyl Phenylalanine

Cai,

Wang,

Zhao

et al. 2024

J. Agric. Food Chem.

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To satisfy the demands of the food industry, innovative flavor enhancers need to be developed urgently to increase the food flavor. In our work, N-lauroyl phenylalanine (LP) was prepared from phenylalanine (l-Phe) and lauric acid (Lau) in water through the use of commercial enzymes (Promatex, Sumizyme FP-G, and Trypsin), and its flavor-presenting properties and mechanism were investigated. The highest LP yields obtained under one-factor optimized conditions were 61.28, 63.43, and 77.58%, respectively. Sensory assessment and an e-tongue test revealed that 1 mg/L LP enhanced the kokumi, saltiness, and umami of the simulated chicken broth solution and attenuated the bitterness of the l-isoleucine solution. The molecular simulation results suggested that the mechanisms of LP enhancement of kokumi and umami were related to hCaSR and hT1R1–hT1R3, and that hydrophobic forces and hydrogen bonds were involved in the binding of LP to taste receptors. The results implied that LP is a potential flavor enhancer for food applications.

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Section: Nmr Characterization Of Lpmentioning

confidence: 98%

A Novel Compound with Kokumi Properties: Enzymatic Preparation and Taste Presentation Evaluation of N-Lauroyl Phenylalanine

Cai,

Wang,

Zhao

et al. 2024

J. Agric. Food Chem.

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“…However, given that viruses do not themselves produce the same repertoire of metabolites compared with bacteria and fungi, it is harder to speculate how viruses could activate taste receptors. However, because peptides can be T2R agonists [ 30 , 297 ] or blockers [ 286 , 298 , 299 ], it is in theory possible that viral proteins can activate one or more taste receptors. It may also be that taste receptors detect metabolites released by cells during viral replication or budding or during viral-induced apoptosis.…”

Section: Conclusion and Remaining Questionsmentioning

confidence: 99%

Interkingdom Detection of Bacterial Quorum-Sensing Molecules by Mammalian Taste Receptors

Kouakou

Lee

2023

Microorganisms

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Bitter and sweet taste G protein-coupled receptors (known as T2Rs and T1Rs, respectively) were originally identified in type II taste cells on the tongue, where they signal perception of bitter and sweet tastes, respectively. Over the past ~15 years, taste receptors have been identified in cells all over the body, demonstrating a more general chemosensory role beyond taste. Bitter and sweet taste receptors regulate gut epithelial function, pancreatic β cell secretion, thyroid hormone secretion, adipocyte function, and many other processes. Emerging data from a variety of tissues suggest that taste receptors are also used by mammalian cells to “eavesdrop” on bacterial communications. These receptors are activated by several quorum-sensing molecules, including acyl-homoserine lactones and quinolones from Gram-negative bacteria such as Pseudomonas aeruginosa, competence stimulating peptides from Streptococcus mutans, and D-amino acids from Staphylococcus aureus. Taste receptors are an arm of immune surveillance similar to Toll-like receptors and other pattern recognition receptors. Because they are activated by quorum-sensing molecules, taste receptors report information about microbial population density based on the chemical composition of the extracellular environment. This review summarizes current knowledge of bacterial activation of taste receptors and identifies important questions remaining in this field.

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“…Among which, 8 peptides (SC, DM, SM, CR, DSW, CQR, CGSR, and KPTW) were non-toxic in the toxicity prediction. The '-CDOCKER_ENERGY' values reflected the bingding affinity between the T2R14 receptor and the peptides [9] . Eight peptides (SC, DM, SM, CR, DSW, CQR, CGSR, and KPTW) were used for the molecular docking, and their '-CDOCKER_ENERGY' values were 152.…”

Section: Virtual Screening Of Potential Bitter Receptor T2r14 Blockin...mentioning

confidence: 99%

“…However, only a few blockers have been identified that can against specific T2Rs on a receptor level [3] . Currently, bioactive peptides have attracted much attention and are widely applied in the food industry, chemistry and biology with the advantages of safety, slight side-effects, diverse functions and selectivity [9] . The peptide QRPR from myosin of Mizuhopecten yessoensis was demonstrated as the potential candidate for suppressing bitterness [10] .…”

Section: Introductionmentioning

confidence: 99%

Identification of bitter receptor T2R14 blocking peptides from egg protein via virtual screening and molecular docking

Zhao,

Zhang,

Wang

et al. 2023

Food Science of Animal Products

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Bitter taste receptors (T2Rs) perform crucial role in the sensation of bitterness, especially the T2R14 that can widely perceive the bitterness. In this study, egg protein-derived T2R14 blocking peptides were identified using physicochemical property prediction, molecular docking, molecular dynamic simulation, and in vitro validation. The '-CDOCKER_ENERGY' values of peptides CQR and CGSR were higher than the positive control LEGSLE, were 314.26 and 294.85 kJ/mol, respectively. The results showed that the half inhibitory concentration (IC 50 ) of the egg protein-derived peptides CQR and CGSR were 382.87 and 370.13 μmol/L, respectively, and higher than that of the positive control LEGSLE. The molecular docking results showed that the conventional hydrogen bond interaction was the main binding force between T2R14 and peptides (i.e., CQR and CGSR). In summary, the novel T2R14 blocking peptides CQR and CGSR were identified, and aided in understanding the mechanism responsible for T2R14 blocking peptides. This study provides further guidance to block T2R14 and may address the bitterness problem in the food industry.

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Identification and molecular docking of peptides from Mizuhopecten yessoensis myosin as human bitter taste receptor T2R14 blockers

Abstract: Bitter taste receptor 14(T2R14) is one of the most widely regulated bitter taste Receptors(T2Rs), and plays a vital role in the research of T2Rs blockers. In this study, potential T2R14...

Cited by 11 publications

References 29 publications

A Novel Compound with Kokumi Properties: Enzymatic Preparation and Taste Presentation Evaluation of N-Lauroyl Phenylalanine

A Novel Compound with Kokumi Properties: Enzymatic Preparation and Taste Presentation Evaluation of N-Lauroyl Phenylalanine

Interkingdom Detection of Bacterial Quorum-Sensing Molecules by Mammalian Taste Receptors

Identification of bitter receptor T2R14 blocking peptides from egg protein via virtual screening and molecular docking

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