Cargando…
Taste peptides derived from Stropharia rugosoannulata fermentation mycelium and molecular docking to the taste receptor T1R1/T1R3
This study identified the peptides in the fermentation mycelia of Stropharia rugosoannulata. The molecular weight of the peptides was below 3,000 Da. Heptapeptides to decapeptides were the main peptides in the fermentation mycelia of S. rugosoannulata. More than 50% of the peptides had salty and uma...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9371610/ https://www.ncbi.nlm.nih.gov/pubmed/35967776 http://dx.doi.org/10.3389/fnut.2022.960218 |
_version_ | 1784767194138148864 |
---|---|
author | Li, Wen Chen, Wanchao Wu, Di Zhang, Zhong Yang, Yan |
author_facet | Li, Wen Chen, Wanchao Wu, Di Zhang, Zhong Yang, Yan |
author_sort | Li, Wen |
collection | PubMed |
description | This study identified the peptides in the fermentation mycelia of Stropharia rugosoannulata. The molecular weight of the peptides was below 3,000 Da. Heptapeptides to decapeptides were the main peptides in the fermentation mycelia of S. rugosoannulata. More than 50% of the peptides had salty and umami taste characteristics, and the long-chain peptides (decapeptides to 24 peptides) also played an essential role in the pleasant taste characteristics of mycelium. In the salty and umami peptide of S. rugosoannulata, the distribution of non-polar hydrophobic amino acids and polar-uncharged amino acids accounted for a relatively high proportion, and the proportion of polar-uncharged amino acids further increased, with the extension of the peptide chain. P, F, I, l, V, G, S, T, and D were the amino acids with a high proportion in the peptides. The taste peptides can bind to more than 60% of the active amino acid residues in the cavity-binding domain of the T1R1/T1R3 receptors. Hydrogen bond interaction was the primary mode of interaction between the peptides and the receptor. The first and second amino acid residues (such as S, V, E, K, G, and A) at the C-terminal and N-terminal of the peptides were easy to bind to T1R1/T1R3 receptors. Asp108, Asn150, Asp147, Glu301, Asp219, Asp243, Glu70, Asp218 in T1R1, and Glu45, Glu148, Glu301, Glu48, and Ala46 in TIR3 were the key active amino acid sites of taste peptides binding to T1R1/T1R3 receptors. |
format | Online Article Text |
id | pubmed-9371610 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-93716102022-08-12 Taste peptides derived from Stropharia rugosoannulata fermentation mycelium and molecular docking to the taste receptor T1R1/T1R3 Li, Wen Chen, Wanchao Wu, Di Zhang, Zhong Yang, Yan Front Nutr Nutrition This study identified the peptides in the fermentation mycelia of Stropharia rugosoannulata. The molecular weight of the peptides was below 3,000 Da. Heptapeptides to decapeptides were the main peptides in the fermentation mycelia of S. rugosoannulata. More than 50% of the peptides had salty and umami taste characteristics, and the long-chain peptides (decapeptides to 24 peptides) also played an essential role in the pleasant taste characteristics of mycelium. In the salty and umami peptide of S. rugosoannulata, the distribution of non-polar hydrophobic amino acids and polar-uncharged amino acids accounted for a relatively high proportion, and the proportion of polar-uncharged amino acids further increased, with the extension of the peptide chain. P, F, I, l, V, G, S, T, and D were the amino acids with a high proportion in the peptides. The taste peptides can bind to more than 60% of the active amino acid residues in the cavity-binding domain of the T1R1/T1R3 receptors. Hydrogen bond interaction was the primary mode of interaction between the peptides and the receptor. The first and second amino acid residues (such as S, V, E, K, G, and A) at the C-terminal and N-terminal of the peptides were easy to bind to T1R1/T1R3 receptors. Asp108, Asn150, Asp147, Glu301, Asp219, Asp243, Glu70, Asp218 in T1R1, and Glu45, Glu148, Glu301, Glu48, and Ala46 in TIR3 were the key active amino acid sites of taste peptides binding to T1R1/T1R3 receptors. Frontiers Media S.A. 2022-07-28 /pmc/articles/PMC9371610/ /pubmed/35967776 http://dx.doi.org/10.3389/fnut.2022.960218 Text en Copyright © 2022 Li, Chen, Wu, Zhang and Yang. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Nutrition Li, Wen Chen, Wanchao Wu, Di Zhang, Zhong Yang, Yan Taste peptides derived from Stropharia rugosoannulata fermentation mycelium and molecular docking to the taste receptor T1R1/T1R3 |
title | Taste peptides derived from Stropharia rugosoannulata fermentation mycelium and molecular docking to the taste receptor T1R1/T1R3 |
title_full | Taste peptides derived from Stropharia rugosoannulata fermentation mycelium and molecular docking to the taste receptor T1R1/T1R3 |
title_fullStr | Taste peptides derived from Stropharia rugosoannulata fermentation mycelium and molecular docking to the taste receptor T1R1/T1R3 |
title_full_unstemmed | Taste peptides derived from Stropharia rugosoannulata fermentation mycelium and molecular docking to the taste receptor T1R1/T1R3 |
title_short | Taste peptides derived from Stropharia rugosoannulata fermentation mycelium and molecular docking to the taste receptor T1R1/T1R3 |
title_sort | taste peptides derived from stropharia rugosoannulata fermentation mycelium and molecular docking to the taste receptor t1r1/t1r3 |
topic | Nutrition |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9371610/ https://www.ncbi.nlm.nih.gov/pubmed/35967776 http://dx.doi.org/10.3389/fnut.2022.960218 |
work_keys_str_mv | AT liwen tastepeptidesderivedfromstrophariarugosoannulatafermentationmyceliumandmoleculardockingtothetastereceptort1r1t1r3 AT chenwanchao tastepeptidesderivedfromstrophariarugosoannulatafermentationmyceliumandmoleculardockingtothetastereceptort1r1t1r3 AT wudi tastepeptidesderivedfromstrophariarugosoannulatafermentationmyceliumandmoleculardockingtothetastereceptort1r1t1r3 AT zhangzhong tastepeptidesderivedfromstrophariarugosoannulatafermentationmyceliumandmoleculardockingtothetastereceptort1r1t1r3 AT yangyan tastepeptidesderivedfromstrophariarugosoannulatafermentationmyceliumandmoleculardockingtothetastereceptort1r1t1r3 |