Molecular Recognition and Modification Strategies of Umami Dipeptides with T1R1/T1R3 Receptors
Umami is a fundamental taste sensation, often described as a delicious and pleasant flavor perception. To enhance or complement the original flavor and meet the tastes of diverse regions, umami dipeptides have been extensively utilized in global food manufacturing. Currently, the application and pur...
Saved in:
| Main Authors: | , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-06-01
|
| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/30/13/2774 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849704644029186048 |
|---|---|
| author | Kaixuan Hu Guangzhou Sun Wentong Yu Mengyu Zhang Shuang Wang Yujie Cao Dongling Hu Li Liang Gang He Jianping Hu Wei Liu |
| author_facet | Kaixuan Hu Guangzhou Sun Wentong Yu Mengyu Zhang Shuang Wang Yujie Cao Dongling Hu Li Liang Gang He Jianping Hu Wei Liu |
| author_sort | Kaixuan Hu |
| collection | DOAJ |
| description | Umami is a fundamental taste sensation, often described as a delicious and pleasant flavor perception. To enhance or complement the original flavor and meet the tastes of diverse regions, umami dipeptides have been extensively utilized in global food manufacturing. Currently, the application and purification techniques of dipeptides are relatively mature, while their umami mechanisms and molecular modification are both scarce. In this work, the 3D structure of the umami dipeptide target T1R1/T1R3 was first obtained through sequence alignment and homology modeling, then followed by the successful construction of a database containing 400 samples of dipeptides. Subsequently, the complex models of T1R1/T1R3, respectively, with DG (Asp-Gly) and EK (Glu-Lys) (i.e., T1R1_DG/T1R3, T1R1/T1R3_DG, T1R1_EK/T1R3, and T1R1/T1R3_EK) were obtained via molecular docking and virtual screening. Finally, based on comparative molecular dynamics (MD) simulation trajectories, the binding free energy was calculated to investigate receptor–ligand recognition and conformational changes, providing some implications for potential modifications of umami dipeptides. T1R1 tends to bind relatively small umami dipeptides, whereas T1R3 does the opposite, both of which favor the recognition of acidic and hydrophilic dipeptides. By comparing strategies such as hydroxyl introduction and chain length alteration, electrostatic effects may be more important than non-polar effects in molecular design. This work not only explores the recognition mechanism of umami dipeptides with the receptor T1R1/T1R3 showing certain theoretical significance, but also provides feasible suggestions for dipeptide screening and modification having certain application value. |
| format | Article |
| id | doaj-art-890ca8a718ec4a9c839ee9093cbebc2a |
| institution | DOAJ |
| issn | 1420-3049 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj-art-890ca8a718ec4a9c839ee9093cbebc2a2025-08-20T03:16:42ZengMDPI AGMolecules1420-30492025-06-013013277410.3390/molecules30132774Molecular Recognition and Modification Strategies of Umami Dipeptides with T1R1/T1R3 ReceptorsKaixuan Hu0Guangzhou Sun1Wentong Yu2Mengyu Zhang3Shuang Wang4Yujie Cao5Dongling Hu6Li Liang7Gang He8Jianping Hu9Wei Liu10Bamboo & Forest Institute of Science, Technology and Industrial Innovation, Leshan Normal University, Leshan 614004, ChinaKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu 610106, ChinaKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu 610106, ChinaKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu 610106, ChinaKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu 610106, ChinaKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu 610106, ChinaKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu 610106, ChinaKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu 610106, ChinaKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu 610106, ChinaKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu 610106, ChinaBamboo & Forest Institute of Science, Technology and Industrial Innovation, Leshan Normal University, Leshan 614004, ChinaUmami is a fundamental taste sensation, often described as a delicious and pleasant flavor perception. To enhance or complement the original flavor and meet the tastes of diverse regions, umami dipeptides have been extensively utilized in global food manufacturing. Currently, the application and purification techniques of dipeptides are relatively mature, while their umami mechanisms and molecular modification are both scarce. In this work, the 3D structure of the umami dipeptide target T1R1/T1R3 was first obtained through sequence alignment and homology modeling, then followed by the successful construction of a database containing 400 samples of dipeptides. Subsequently, the complex models of T1R1/T1R3, respectively, with DG (Asp-Gly) and EK (Glu-Lys) (i.e., T1R1_DG/T1R3, T1R1/T1R3_DG, T1R1_EK/T1R3, and T1R1/T1R3_EK) were obtained via molecular docking and virtual screening. Finally, based on comparative molecular dynamics (MD) simulation trajectories, the binding free energy was calculated to investigate receptor–ligand recognition and conformational changes, providing some implications for potential modifications of umami dipeptides. T1R1 tends to bind relatively small umami dipeptides, whereas T1R3 does the opposite, both of which favor the recognition of acidic and hydrophilic dipeptides. By comparing strategies such as hydroxyl introduction and chain length alteration, electrostatic effects may be more important than non-polar effects in molecular design. This work not only explores the recognition mechanism of umami dipeptides with the receptor T1R1/T1R3 showing certain theoretical significance, but also provides feasible suggestions for dipeptide screening and modification having certain application value.https://www.mdpi.com/1420-3049/30/13/2774umami dipeptideT1R1/T1R3molecular dynamics simulationmolecular recognitionmolecular modification |
| spellingShingle | Kaixuan Hu Guangzhou Sun Wentong Yu Mengyu Zhang Shuang Wang Yujie Cao Dongling Hu Li Liang Gang He Jianping Hu Wei Liu Molecular Recognition and Modification Strategies of Umami Dipeptides with T1R1/T1R3 Receptors Molecules umami dipeptide T1R1/T1R3 molecular dynamics simulation molecular recognition molecular modification |
| title | Molecular Recognition and Modification Strategies of Umami Dipeptides with T1R1/T1R3 Receptors |
| title_full | Molecular Recognition and Modification Strategies of Umami Dipeptides with T1R1/T1R3 Receptors |
| title_fullStr | Molecular Recognition and Modification Strategies of Umami Dipeptides with T1R1/T1R3 Receptors |
| title_full_unstemmed | Molecular Recognition and Modification Strategies of Umami Dipeptides with T1R1/T1R3 Receptors |
| title_short | Molecular Recognition and Modification Strategies of Umami Dipeptides with T1R1/T1R3 Receptors |
| title_sort | molecular recognition and modification strategies of umami dipeptides with t1r1 t1r3 receptors |
| topic | umami dipeptide T1R1/T1R3 molecular dynamics simulation molecular recognition molecular modification |
| url | https://www.mdpi.com/1420-3049/30/13/2774 |
| work_keys_str_mv | AT kaixuanhu molecularrecognitionandmodificationstrategiesofumamidipeptideswitht1r1t1r3receptors AT guangzhousun molecularrecognitionandmodificationstrategiesofumamidipeptideswitht1r1t1r3receptors AT wentongyu molecularrecognitionandmodificationstrategiesofumamidipeptideswitht1r1t1r3receptors AT mengyuzhang molecularrecognitionandmodificationstrategiesofumamidipeptideswitht1r1t1r3receptors AT shuangwang molecularrecognitionandmodificationstrategiesofumamidipeptideswitht1r1t1r3receptors AT yujiecao molecularrecognitionandmodificationstrategiesofumamidipeptideswitht1r1t1r3receptors AT donglinghu molecularrecognitionandmodificationstrategiesofumamidipeptideswitht1r1t1r3receptors AT liliang molecularrecognitionandmodificationstrategiesofumamidipeptideswitht1r1t1r3receptors AT ganghe molecularrecognitionandmodificationstrategiesofumamidipeptideswitht1r1t1r3receptors AT jianpinghu molecularrecognitionandmodificationstrategiesofumamidipeptideswitht1r1t1r3receptors AT weiliu molecularrecognitionandmodificationstrategiesofumamidipeptideswitht1r1t1r3receptors |