期刊
BIOMATERIALS
卷 281, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.biomaterials.2021.121338
关键词
Umami peptides; Quantum chemical simulations; Molecular docking; Binding modes; A novel decision rule for umami peptides
资金
- National Natural Science Foundation of China [31972198, 31901813, 32001824, 32172332]
This study analyzed the sequence and properties of umami peptides, and investigated their active sites and binding residues with the receptor T1R1/T1R3. The results identified the key active sites as well as the crucial residues in the receptor that bind umami peptides. A decision rule was proposed to predict potential umami peptides, providing convenience and efficiency.
Umami, providing amino acids/peptides for animal growth, represents one of the major attractive taste mo-dalities. The biochemical and umami properties of peptide are both important for scientific research and food industry. In this study, we did the sequence analysis of 205 umami peptides with 2-18 amino acids, sought the active sites of umami peptides by quantum chemical simulations and investigated their recognition residues with receptor T1R1/T1R3 by molecular docking. The results showed the peptides with 2-3 amino acids accounting for 44% of the total umami peptides. Residues D and E are the key active sites no matter where they are in the peptides (N-terminal, C-terminal or middle), when umami peptides contain D/E residues. N69, D147, R151, A170, S172, S276 and R277 residues in T1R1 receptor were deemed to be the key residues binding umami peptides. Finally, a powerful decision rule for umami peptides was proposed to predict potential umami peptides, which was convenient and efficient.
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