Efficient screening and discovery of umami peptides in Douchi enhanced by molecular dynamics simulations
In this study, a partial least squares discriminant analysis (PLS-DA) discriminant model for umami peptides was constructed based on molecular dynamics simulation data, achieving a R2 value of 0.949 and a Q2 value of 0.558. Using this novel model and bioinformatics screening methods, five new umami...
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| Format: | Article |
| Language: | English |
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Elsevier
2024-12-01
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| Series: | Food Chemistry: X |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590157524008289 |
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| author | Weidan Guo Kangzi Ren Zhao Long Xiangjin Fu Jianan Zhang Min Liu Yaquan Chen |
| author_facet | Weidan Guo Kangzi Ren Zhao Long Xiangjin Fu Jianan Zhang Min Liu Yaquan Chen |
| author_sort | Weidan Guo |
| collection | DOAJ |
| description | In this study, a partial least squares discriminant analysis (PLS-DA) discriminant model for umami peptides was constructed based on molecular dynamics simulation data, achieving a R2 value of 0.949 and a Q2 value of 0.558. Using this novel model and bioinformatics screening methods, five new umami peptides (EALEATAQ, SPPTEE, SEEG, KEE, and FEE, with umami taste thresholds of 0.139, 0.085, 0.096, 0.060, and 0.079 mg/mL, respectively) were identified in Douchi. Molecular docking revealed that the residues ASN150 of T1R1, as well as SER170, GLU301 and GLN389 of T1R3, might be key amino acid residues for the binding of umami peptides to T1R1/T1R3. Molecular dynamics simulations revealed significant differences in the root-mean-square fluctuation (RMSF) values between the two complex systems of umami peptides-T1R1/T1R3 and non-umami peptides-T1R1/T1R3. The newly constructed umami peptide discriminant model can improve the accuracy of umami peptide screening and enhance the efficiency of discovering new umami peptides. |
| format | Article |
| id | doaj-art-a2b3cc9327f54cf2ad400ae2678f5909 |
| institution | OA Journals |
| issn | 2590-1575 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: X |
| spelling | doaj-art-a2b3cc9327f54cf2ad400ae2678f59092025-08-20T02:38:23ZengElsevierFood Chemistry: X2590-15752024-12-012410194010.1016/j.fochx.2024.101940Efficient screening and discovery of umami peptides in Douchi enhanced by molecular dynamics simulationsWeidan Guo0Kangzi Ren1Zhao Long2Xiangjin Fu3Jianan Zhang4Min Liu5Yaquan Chen6College of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, ChinaCollege of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, ChinaCollege of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China; Corresponding author.College of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China; Seasonings Green Manufacturing Engineering Technology Research Center of Hunan Province, Hun an Huixiangxuan Bio. Tech. Ltd. Com., Liuyang 410323, China; Corresponding author at: College of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China.College of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, ChinaSeasonings Green Manufacturing Engineering Technology Research Center of Hunan Province, Hun an Huixiangxuan Bio. Tech. Ltd. Com., Liuyang 410323, ChinaHunan Xiangdian Food Ltd. Com, Liuyang 410301, ChinaIn this study, a partial least squares discriminant analysis (PLS-DA) discriminant model for umami peptides was constructed based on molecular dynamics simulation data, achieving a R2 value of 0.949 and a Q2 value of 0.558. Using this novel model and bioinformatics screening methods, five new umami peptides (EALEATAQ, SPPTEE, SEEG, KEE, and FEE, with umami taste thresholds of 0.139, 0.085, 0.096, 0.060, and 0.079 mg/mL, respectively) were identified in Douchi. Molecular docking revealed that the residues ASN150 of T1R1, as well as SER170, GLU301 and GLN389 of T1R3, might be key amino acid residues for the binding of umami peptides to T1R1/T1R3. Molecular dynamics simulations revealed significant differences in the root-mean-square fluctuation (RMSF) values between the two complex systems of umami peptides-T1R1/T1R3 and non-umami peptides-T1R1/T1R3. The newly constructed umami peptide discriminant model can improve the accuracy of umami peptide screening and enhance the efficiency of discovering new umami peptides.http://www.sciencedirect.com/science/article/pii/S2590157524008289DouchiPeptidomicsMolecular dockingMolecular dynamics simulationUmami peptide |
| spellingShingle | Weidan Guo Kangzi Ren Zhao Long Xiangjin Fu Jianan Zhang Min Liu Yaquan Chen Efficient screening and discovery of umami peptides in Douchi enhanced by molecular dynamics simulations Food Chemistry: X Douchi Peptidomics Molecular docking Molecular dynamics simulation Umami peptide |
| title | Efficient screening and discovery of umami peptides in Douchi enhanced by molecular dynamics simulations |
| title_full | Efficient screening and discovery of umami peptides in Douchi enhanced by molecular dynamics simulations |
| title_fullStr | Efficient screening and discovery of umami peptides in Douchi enhanced by molecular dynamics simulations |
| title_full_unstemmed | Efficient screening and discovery of umami peptides in Douchi enhanced by molecular dynamics simulations |
| title_short | Efficient screening and discovery of umami peptides in Douchi enhanced by molecular dynamics simulations |
| title_sort | efficient screening and discovery of umami peptides in douchi enhanced by molecular dynamics simulations |
| topic | Douchi Peptidomics Molecular docking Molecular dynamics simulation Umami peptide |
| url | http://www.sciencedirect.com/science/article/pii/S2590157524008289 |
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