AI Chat Paper
Discover the SciOpen Platform and Achieve Your Research Goals with Ease.
Search articles, authors, keywords, DOl and etc.
{{expandStatus?'Exit ':''}}Advanced Search
The taste presentation and receptor perception mechanism of the salty peptide of Stropharia rugosoannulata were predicted and verified using peptide omics and molecular interaction techniques. The combination of aspartic acid (D) and glutamic acid (E), or peptide fragments composed of arginine (R), constitute the characteristic taste structural basis of salty peptides of S. rugosoannulata. The taste intensity of the salty peptide positively correlates with its concentration within a specific concentration range (0.25–1.0 mg/mL). The receptor more easily recognizes the first amino acid residue at the N-terminal of salty peptides and the aspartic acid residue in the peptides. GLU513, ASP707, and VAL508 are the critical amino acid residues for the receptor to recognize salty peptides. TRPV1 is specifically the receptor for recognizing salty peptides. Hydrogen bonds and electrostatic interactions are the main driving forces for the interactions between salty peptides and TRPV1 receptors. KSWDDFFTR has the most potent binding capacity with the receptor and has tremendous potential for application in sodium salt substitution. This study confirmed the taste receptor that specifically recognizes salty peptides, analyzed the receptor-peptide binding interaction, and provided a new idea for understanding the taste receptor perception of salty peptides.
A. Schindler, A. Dunkel, F. Stahler, et al., Discovery of salt taste enhancing arginyl dipeptides in protein digests and fermented fish sauces by means of a sensomics approach, J. Agric. Food Chem. 59 (2011) 12578-12588. https://doi.org/10.1021/jf2041593.
M. Tamura, T. Nakatsuka, M. Tada, et al., The Relationship between taste and primary structure of delicious peptide (Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala) from beef soup, Agric. Biol. Chem. 53 (1989) 319-325.
M.Z. Zhuang, L.Z. Lin, M.M. Zhao, et al., Sequence, taste and umami-enhancing effect of the peptides separated from soy sauce, Food Chem. 206 (2016) 174-181. https://doi.org/10.1016/j.foodchem.2016.03.058.
Y.Y. Zheng, L. Tang, M.G. Yu, et al., Fractionation and identification of salty peptides from yeast extract, J. Food Sci. Technol. 58 (2021) 1199-1208. https://doi.org/10.1007/s13197-020-04836-1.
D.Y. Shen, F. Pan, Z.C. Yang, et al., Identification of novel saltiness-enhancing peptides from yeast extract and their mechanism of action for transmembrane channel-like 4 (TMC4) protein through experimental and integrated computational modeling, Food Chem. 388 (2022) 132993. https://doi.org/10.1016/j.foodchem.2022.132993.
X.Z. Xia, Y. Fu, L. Ma, et al., Protein hydrolysates from Pleurotus geesteranus modified by Bacillus amyloliquefaciens gamma-glutamyl transpeptidase exhibit a remarkable taste-enhancing effect, J. Agric. Food Chem. 70 (2022) 12143-12155. https://doi.org/10.1021/acs.jafc.2c03941.
Y.P. Chen, M.N. Wang, I. Blank, et al., Saltiness-enhancing peptides isolated from the Chinese commercial fermented soybean curds with potential applications in salt reduction, J. Agric. Food Chem. 69 (2021) 10272-10280. https://doi.org/10.1021/acs.jafc.1c03431.
Y. Kong, L.L. Zhang, J. Zhao, et al., Isolation and identification of the umami peptides from shiitake mushroom by consecutive chromatography and LC-Q-TOF-MS, Food Res. Int. 121 (2019) 463-470. https://doi.org/10.1016/j.foodres.2018.11.060.
Y. Zhang, X.C. Gao, D.D. Pan, et al., Isolation, characterization and molecular docking of novel umami and umami-enhancing peptides from Ruditapes philippinarum, Food Chem. 343 (2021) 128522. https://doi.org/10.1016/j.foodchem.2020.128522.
Y. Bu, Y.N. Liu, H.W. Luan, et al., Characterization and structure-activity relationship of novel umami peptides isolated from Thai fish sauce, Food Funct. 12 (2021) 5027-5037. https://doi.org/10.1039/d0fo03326j.
Y.Z. Xiong, X.C. Gao, D.D. Pan, et al., A strategy for screening novel umami dipeptides based on common feature pharmacophore and molecular docking, Biomaterials 288 (2022) 121697. https://doi.org/10.1016/j.biomaterials.2022.121697.
X.P. Li, X.X. Xie, J.X. Wang, et al., Identification, taste characteristics and molecular docking study of novel umami peptides derived from the aqueous extract of the clam meretrix meretrix Linnaeus, Food Chem. 312 (2020) 126053. https://doi.org/10.1016/j.foodchem.2019.126053.
W.Z. Zhao, L.J. Su, S.T. Huo, et al., Virtual screening, molecular docking and identification of umami peptides derived from Oncorhynchus mykiss, Food Sci. Hum. Wellness 12 (2023) 89-93. https://doi.org/10.1016/j.fshw.2022.07.026.
W.H. Zhu, W. He, F. Wang, et al., Prediction, molecular docking and identification of novel umami hexapeptides derived from Atlantic cod (Gadus morhua), Int. J. Food Sci. Tech. 56 (2020) 402-412. https://doi.org/10.1111/ijfs.14655.
Z.P. Yu, L.X. Kang, W.Z. 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.
H. Salehabadi, K. Khajeh, B. Dabirmanesh, et al., Evaluation of angiotensin converting enzyme inhibitors by SPR biosensor and theoretical studies, Enzyme Microb. Technol. 120 (2019) 117-123. https://doi.org/10.1016/j.enzmictec.2018.10.010.
C.X. Zhang, Y.L. Miao, Y.H. Feng, et al., Umami polypeptide detection system targeting the human T1R1 receptor and its taste-presenting mechanism, Biomaterials 287 (2022) 121660. https://doi.org/10.1016/j.biomaterials.2022.121660.
J.J. Gao, P. Chu, C.G. Liu, et al., Discovery and biological evaluation of a small-molecule inhibitor of CRM1 that suppresses the growth of triple-negative breast cancer cells, Traffic 22 (2021) 221-229. https://doi.org/10.1111/tra.12802.
C. Chen, T.Y, Zhu, X.Q. Liu, et al., Identification of a novel PHGDH covalent inhibitor by chemical proteomics and phenotypic profiling, Acta Pharm. Sin. B. 12 (2022) 246-261. https://doi.org/10.1016/j.apsb.2021.06.0082211-3835.
F.Q. Hao, M.M. Tian, X.B. Zhang, et al., Butyrate enhances CPT1A activity to promote fatty acid oxidation and iTreg differentiation, Proc. Natl. Acad. Sci. USA. 118 (2021). https://doi.org/10.1073/pnas.2014681118.
D.R. Zhu, C. Chen, X.Q. Liu, et al., Osteosarcoma cell proliferation suppression via SHP-2-mediated inactivation of the JAK/STAT3 pathway by tubocapsenolide A, J. Adv. Res. 34 (2021) 79-91. https://doi.org/10.1016/j.jare.2021.06.004.
B.Y. Zhang, J.B. Liu, H.D. Wen, et al., Structural requirements and interaction mechanisms of ACE inhibitory peptides: molecular simulation and thermodynamics studies on LAPYK and its modified peptides, Food Sci. Hum. Wellness 11 (2022) 1623-1630. https://doi.org/10.1016/i.fshw.2022.06.021.
W. Li, W.C. Chen, H.L. Ma, et al., Structural characterization and angiotensin-converting enzyme (ACE) inhibitory mechanism of Stropharia rugosoannulata mushroom peptides prepared by ultrasound, Ultrason. Sonochem. 88 (2022) 106074. https://doi.org/10.1016/j.ultsonch.2022.106074.
W. Li, W.C. Chen, H.L. Ma, et al., Study on the relationship between structure and taste activity of the umami peptide of Stropharia rugosoannulata prepared by ultrasound, Ultrason. Sonochem. 90 (2022) 106206. https://doi.org/10.1016/j.ultsonch.2022.106206.
J. Chandrashekar, C. Kuhn, Y. Oka, et al., The cells and peripheral representation of sodium taste in mice, Nature 464 (2010) 297-301. https://doi.org/10.1038/nature08783.
T. Katsumata, H. Nakakuki, C. Tokunaga, et al., Effect of Maillard reacted peptides on human salt taste and the amiloride-insensitive salt taste receptor (TRPV1t), Chem. Senses. 33 (2008) 665-680. https://doi.org/10.1093/chemse/bjn033.
J.B. Hedderich, M. Persechino, K. Becker, et al., The pocketome of G-protein-coupled receptors reveals previously untargeted allosteric sites, Nat. Commun. 13 (2022) 2567. https://doi.org/10.1038/s41467-022-29609-6.
P.L. Flanders, C. Contreras-Martel, N.W. Brown, et al., Combined structural analysis and molecular dynamics reveal penicillin-binding protein inhibition mode with β-lactones, ACS Chem. Biol. (2022) 2c00503. https://doi.org/10.1021/acschembio.2c00503.
S.G. Lim, S.E. Seo, S. Jo, eet al., Highly efficient real-time TRPV1 screening methodology for effective drug candidates, ACS Omega 7 (2022) 36441-36447. https://doi.org/10.1021/acsomega.2c04202.
S.O. Oselusi, A.O. Fadaka, G.J. Wyckoff, et al., Computational target-based screening of anti-MRSA natural products reveals potential multitarget mechanisms of action through peptidoglycan synthesis proteins, ACS Omega 7 (2022) 37896-37906. https://doi.org/10.1021/acsomega.2c05061.
P. Zhou, X.L. Yang, X.G. Wang, et al., A pneumonia outbreak associated with a new coronavirus of probable bat origin, Nature 579 (2020) 270-273. https://doi.org/10.1038/s41586-020-2951-z.
X.L. Tian, C. Li, A.L. Huang, et al., Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody, Emerg. Microbes Infec. 9 (2020) 382-385. https://doi.org/10.1080/22221751.2020.1729069.
G.Y. Chen, Y.C. Pan, T.Y. Wu, et al., Potential natural products that target the SARS-CoV-2 spike protein identified by structure-based virtual screening, isothermal titration calorimetry and lentivirus particles pseudotyped (Vpp) infection assay, J. Tradit. Compl. Med. 12 (2022) 73-89. https://doi.org/10.1016/j.jtcme.2021.09.002.
C. Handa, Y. Yamazaki, S. Yonekubo, et al., Evaluating the correlation of binding affinities between isothermal titration calorimetry and fragment molecular orbital method of estrogen receptor beta with diarylpropionitrile (DPN) or DPN derivatives, J. Steroid Biochem. 222 (2022) 106152. https://doi.org/10.1016/j.jsbmb.2022.106152.
994
Views
217
Downloads
4
Crossref
3
Web of Science
3
Scopus
0
CSCD
Altmetrics
This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
京公网安备11010802044758号