Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation
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),...
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| Format: | Article |
| Language: | English |
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Tsinghua University Press
2024-07-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | https://www.sciopen.com/article/10.26599/FSHW.2022.9250190 |
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| author | Wen Li Shuai Sun Wanchao Chen Haile Ma Tingzhao Li Zhong Zhang Di Wu Mengqiu Yan Yan Yang |
| author_facet | Wen Li Shuai Sun Wanchao Chen Haile Ma Tingzhao Li Zhong Zhang Di Wu Mengqiu Yan Yan Yang |
| author_sort | Wen Li |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-2546c6b42b674807a4184955cbc0400c |
| institution | Kabale University |
| issn | 2097-0765 2213-4530 |
| language | English |
| publishDate | 2024-07-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-2546c6b42b674807a4184955cbc0400c2025-01-10T06:56:48ZengTsinghua University PressFood Science and Human Wellness2097-07652213-45302024-07-011342277228810.26599/FSHW.2022.9250190Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulationWen Li0Shuai Sun1Wanchao Chen2Haile Ma3Tingzhao Li4Zhong Zhang5Di Wu6Mengqiu Yan7Yan Yang8Institute of Edible Fungi, Shanghai Academy of Agricultural Sciences, National Engineering Research Center of Edible Fungi, Key Laboratory of Edible Fungi Resources and Utilization (South), Ministry of Agriculture and Rural Affairs, Shanghai 201403, ChinaAmway (Shanghai) Innovation & Science Co., Ltd., Shanghai 201203, ChinaInstitute of Edible Fungi, Shanghai Academy of Agricultural Sciences, National Engineering Research Center of Edible Fungi, Key Laboratory of Edible Fungi Resources and Utilization (South), Ministry of Agriculture and Rural Affairs, Shanghai 201403, ChinaSchool of Food & Biological Engineering, Institute of Food Physical Processing, Jiangsu University, Zhenjiang 212013, ChinaAmway (Shanghai) Innovation & Science Co., Ltd., Shanghai 201203, ChinaInstitute of Edible Fungi, Shanghai Academy of Agricultural Sciences, National Engineering Research Center of Edible Fungi, Key Laboratory of Edible Fungi Resources and Utilization (South), Ministry of Agriculture and Rural Affairs, Shanghai 201403, ChinaInstitute of Edible Fungi, Shanghai Academy of Agricultural Sciences, National Engineering Research Center of Edible Fungi, Key Laboratory of Edible Fungi Resources and Utilization (South), Ministry of Agriculture and Rural Affairs, Shanghai 201403, ChinaInstitute of Edible Fungi, Shanghai Academy of Agricultural Sciences, National Engineering Research Center of Edible Fungi, Key Laboratory of Edible Fungi Resources and Utilization (South), Ministry of Agriculture and Rural Affairs, Shanghai 201403, ChinaInstitute of Edible Fungi, Shanghai Academy of Agricultural Sciences, National Engineering Research Center of Edible Fungi, Key Laboratory of Edible Fungi Resources and Utilization (South), Ministry of Agriculture and Rural Affairs, Shanghai 201403, ChinaThe 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.https://www.sciopen.com/article/10.26599/FSHW.2022.9250190salty peptidemolecular dockingbiolayer interferometryisothermal titration calorimetry |
| spellingShingle | Wen Li Shuai Sun Wanchao Chen Haile Ma Tingzhao Li Zhong Zhang Di Wu Mengqiu Yan Yan Yang Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation Food Science and Human Wellness salty peptide molecular docking biolayer interferometry isothermal titration calorimetry |
| title | Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation |
| title_full | Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation |
| title_fullStr | Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation |
| title_full_unstemmed | Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation |
| title_short | Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation |
| title_sort | exploring the taste presentation and receptor perception mechanism of salty peptides from stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation |
| topic | salty peptide molecular docking biolayer interferometry isothermal titration calorimetry |
| url | https://www.sciopen.com/article/10.26599/FSHW.2022.9250190 |
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