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Food Science of Animal Products 2023, 1(2): 9240021 https://doi.org/10.26599/FSAP.2023.9240021
Research Article | Open Access | Issue | Published: 01 September 2023

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

Show Author's Information Wenzhu Zhao1,  Shanshan Zhang2,  Yingxue Wang3,  Long Ding4,  Zhipeng Yu1( )
School of Food Science and Engineering, Hainan University, Haikou 570228, China
College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China
College of Food Science and Engineering, Bohai University, Jinzhou 121013, China
College of Food Science and Engineering, Northwest A&F University, Yangling 712100, China
Keywords:
molecular docking, molecular dynamic simulation, peptides, egg protein, T2R14 receptor
Cite this article:
Zhao W, Zhang S, Wang Y, et al. Identification of bitter receptor T2R14 blocking peptides from egg protein via virtual screening and molecular docking. Food Science of Animal Products, 2023, 1(2): 9240021. https://doi.org/10.26599/FSAP.2023.9240021
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Abstract Full text About this article

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 (IC50) 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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About this article

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

Show Author's information Wenzhu Zhao1, Shanshan Zhang2, Yingxue Wang3, Long Ding4, Zhipeng Yu1( )
School of Food Science and Engineering, Hainan University, Haikou 570228, China
College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China
College of Food Science and Engineering, Bohai University, Jinzhou 121013, China
College of Food Science and Engineering, Northwest A&F University, Yangling 712100, China

Abstract

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 (IC50) 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.

Keywords: molecular docking, molecular dynamic simulation, peptides, egg protein, T2R14 receptor

References(29)

[1]

J. Upadhyaya, S. P. Pydi, N. Singh, et al., Bitter taste receptor T2R1 is activated by dipeptides and tripeptides, Biochem. Biophys. Res. Commun. 398(2) (2010) 331–335. https://doi.org/10.1016/j.bbrc.2010.06.097.
DOI Google Scholar
[2]

Q. Xu, H. Hong, W. Yu, et al., Sodium chloride suppresses the bitterness of protein hydrolysates by decreasing hydrophobic interactions, J. Food Sci. 84(1/3) (2019) 86–91. https://doi.org/10.1111/1750.3841.14419.
DOI Google Scholar
[3]

C. Zhang, M. Alashi, N. Singh, et al., Beef protein-derived peptides as bitter taste receptor T2R4 blockers, J. Agr. Food Chem. 66(19) (2018) 4902–4912. https://doi.org/10.1021/acs.jafc.8b00830.
DOI Google Scholar
[4]

C. P. Harmon, D. Deng, P. A. Breslin, et al., Bitter taste receptors (T2Rs) are sentinels that coordinate metabolic and immunological defense responses, Curr. Opin. Physiol. 20 (2021) 70–76. https://doi.org/10.1016/j.cophys.2021.01.006.
DOI Google Scholar
[5]
Y. Su, H. Jie, Q. Zhu, et al., Effect of bitter compounds on the expression of bitter taste receptor T2R7 downstream signaling effectors in cT2R7/pDisplay-Gα16/gust44/pcDNA3.1(+) cells, Biomed. Res. Int. (2019) 6301915. https://doi.org/10.1155/2019/6301915.
DOI
[6]

W. S. U. Roland, L. van Buren, H. Gruppen, et al., Bitter taste receptor activation by flavonoids and isoflavonoids: modeled structural requirements for activation of hTAS2R14 and hTAS2R39, J. Agr. Food Chem. 61(44) (2013) 10454–10466. https://doi.org/10.1021/jf403387p.
DOI Google Scholar
[7]

W. Meyerhof, C. Batram, C. Kuhn, et al., The molecular receptive ranges of human TAS2R bitter taste receptors, Chem. Senses. 35(2) (2010) 157–170. https://doi.org/10.1093/chense/bjp092.
DOI Google Scholar
[8]

M. Behrens, A. Brockhoff, C. Kuhn, et al., The human taste receptor hTAS2R14 responds to a variety of different bitter compounds, Biochem. Bioph. Res. Co. 319(2) (2004) 479–485. https://doi.org/10.1016/j.bbrc.2004.05.019.
DOI Google Scholar
[9]

Z. Yu, R. Kan, H. Ji, et al., Identification of tuna protein-derived peptides as potent SARS-CoV-2 inhibitors via molecular docking and molecular dynamic simulation, Food Chem. 342 (2021) 128366. https://doi.org/10.1016/j.foodchem.2020.128336.
DOI Google Scholar
[10]

W. Zhao, D. Li, Y. Wang, et al., Identification and molecular docking of peptides from Mizuhopecten yessoensis myosin as human bitter taste receptor T2R14 blockers, Food Funct. 12(23) (2021) 11966–11973. https://doi.org/10.1039/D1FO02447G.
DOI Google Scholar
[11]

Z. Yu, Y. Wang, W. Zhao, et al., Identification of Oncorhynchus mykiss nebulin-derived peptides as bitter taste receptor TAS2R14 blockers by in silico screening and molecular docking, Food Chem. 368 (2022) 130839. https://doi.org/10.1016/j.foodchem.2021.130839.
DOI Google Scholar
[12]

W. Liao, F. Jahandideh, H. Fan, et al., Chapter one: egg protein-derived bioactive peptides: preparation, efficacy, and absorption, Adv. Food Nutr. Res. 85 (2018) 1–58. https://doi.org/10.1016/bs.afnr.2018.02.001.
DOI Google Scholar
[13]

N. Xiao, Y. Zhao, Y. Yao, et al., Biological activities of egg yolk lipids: a review, J. Agr. Food Chem. 68(7) (2020) 1948–1957. https://doi.org/10.1021/acs.jafc.9b06616.
DOI Google Scholar
[14]

H. Fan, J. Wang, W. Liao, et al., Identification and characterization of gastrointestinal-resistant angiotensin-converting enzyme inhibitory peptides from egg white proteins, J. Agr. Food Chem. 67(25) (2019) 7147–7156. https://doi.org/10.1021/acs.jafc.9b01071.
DOI Google Scholar
[15]

Y. H. Zhang, J. Bai, W. N. Jiang, et al., Promising hen egg-derived proteins/peptides (EDPs) for food engineering, natural products and precision medicines, Res. Vet. Sci. 128 (2020) 153–161. https://doi.org/10.1016/j.rvsc.2019.11.011.
DOI Google Scholar
[16]
Z. Yu, L. Wang, S. Wu, et al., In vivo anti-hypertensive effect of peptides from egg white and its molecular mechanism with ACE, Int. J. Food Sci. Tech. 56(2) (2021) 10303–1039. https://doi.org/10.1111/ijfs.14756.
DOI
[17]

N. Xiao, X. Huang, W. He, et al., A review on recent advances of egg byproducts: preparation, functional properties, biological activities and food applications, Food Res. Int. 147 (2021) 110563. https://doi.org/10.1016/j.foodres.2021.110563.
DOI Google Scholar
[18]

Z. Yu, Y. Fan, W. Zhao, et al., Novel angiotensin-converting enzyme inhibitory peptides derived from oncorhynchus mykiss nebulin: virtual screening and in silico molecular docking study, J. Food Sci. 83(7/9) (2018) 2375–2383. https://doi.org/10.1111/1750-3841.14299.
DOI Google Scholar
[19]

Z. Yu, S. Wu, W. Zhao, et al., Identification of novel angiotensin-I converting enzyme inhibitory peptide from collagen hydrolysates and its molecular inhibitory mechanism, Int. J. Food Sci. Tech. 55(9) (2020) 3145–3152. https://doi.org/10.1111/ijfs.14578.
DOI Google Scholar
[20]

Z. Yu, L. Kang, W. Zhao, et al., Identification of novel umami peptides from myosin via homology modeling and molecular docking, Food Chem. 344 (2021) 128728. https://doi.org/10.1016/j.foodchem.2020.128728.
DOI Google Scholar
[21]

E. Gasteiger, A. Gattiker, C. Hoogland, et al., ExPASy: the proteomics server for in-depth protein knowledge and analysis, Oxford University Press. 31(13) (2003) 3784–3788. https://doi.org/10.1093/nar/gkg563.
DOI Google Scholar
[22]

T. Lafarga, P. O’Connor, M. Hayes, In silico methods to identify meat-derived prolyl endopeptidase inhibitors, Food Chem. 175 (2015) 337–343. https://doi.org/10.1016/j.foodchem.2014.11.150.
DOI Google Scholar
[23]
E. Martz, Protein Data Bank (PDB), John. Wiley & Sons, Inc. 2004. https://doi.org/10.1007/978-1-4020-6754-9_13596.
DOI
[24]

Q. Xu, N. Singh, H. Hong, et al., Hen protein-derived peptides as the blockers of human bitter taste receptors T2R4, T2R7 and T2R14, Food Chem. 283 (2019) 621–627. https://doi.org/10.1016/j.foodchem.2019.01.059.
DOI Google Scholar
[25]

M. J. Abraham, T. Murtola, R. Schulz, et al., GROMACS: high performance molecular simulations through multi-level parallelism from laptops to supercomputers, Software X 1/2 (2015) 19–25. https://doi.org/10.1016/j.softx.2015.06.001.
DOI Google Scholar
[26]

B. R. Brooks, C. L. Brooks, A. D. Mackerell, et al., CHARMM: the biomolecular simulation program, J. Comput. Chem. 30(10) (2019) 1545–1614. https://doi.org/10.1002/jcc.21287.
DOI Google Scholar
[27]

E. G. D. Santos, R. X. Faria, C. R. Rodrigues, et al., Molecular dynamic simulations of full-length human purinergic receptor subtype P2X7 bonded to potent inhibitors, Eur. J. Pharm. Sci. 152 (2020) 105454. https://doi.org/10.1016/j.ejps.2020.105454.
DOI Google Scholar
[28]

S. Song, J. Zhuang, C. Ma, et al., Identification of novel umami peptides from Boletus edulis and its mechanism via sensory analysis and molecular simulation approaches, Food Chem. 398 (2023) 133835. https://doi.org/10.1016/j.foodchem.2022.133835.
DOI Google Scholar
[29]
Z. Liang, H. Li, X. Lu, et al., 3D-QSAR, in vitro assay and MD simulations studies on the design, bioactivities and different inhibitory modes of the novel DPP-IV inhibitory peptides, J. Mol. Struct. 1283 (2023) 135271. https://doi.org/10.1016/j.molstruc.2023.135271.
DOI
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Publication history

Received: 22 May 2023
Revised: 13 June 2023
Accepted: 05 July 2023
Published: 01 September 2023
Issue date: June 2023

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© Beijing Academy of Food Sciences 2023.

Acknowledgements

Acknowledgements

This study was supported by the National Key Research and Development Program of China (2018YFD0400301).

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Food Science of Animal Products published by Tsinghua University Press. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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