Structural requirements and interaction mechanisms of ACE inhibitory peptides: molecular simulation and thermodynamics studies on LAPYK and its modified peptides
The understanding of the structural requirements and the intermolecular-interaction mechanism are important for discovering potent angiotensin-converting enzyme (ACE) inhibitory peptides. In this study, we modified an egg-white derived peptide, LAPYK, using the amino acids with different properties...
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| Format: | Article |
| Language: | English |
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Tsinghua University Press
2022-11-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453022001045 |
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| author | Biying Zhang Jingbo Liu Hedi Wen Feng Jiang Erlei Wang Ting Zhang |
| author_facet | Biying Zhang Jingbo Liu Hedi Wen Feng Jiang Erlei Wang Ting Zhang |
| author_sort | Biying Zhang |
| collection | DOAJ |
| description | The understanding of the structural requirements and the intermolecular-interaction mechanism are important for discovering potent angiotensin-converting enzyme (ACE) inhibitory peptides. In this study, we modified an egg-white derived peptide, LAPYK, using the amino acids with different properties to produce the LAPYK-modified peptides. The ACE inhibitory activities of the modified peptides were determined to explore the structural requirements of ACE inhibitory peptides (ACEIPs). Molecular simulation and isothermal titration calorimetry analysis were used to investigate interactions between the peptides and ACE. We found that hydrophobicity and the amino acids with ring structures were beneficial for the ACE inhibitory activities of the peptides. The results of the molecular mechanics poisson boltzmann surface area (MMPBSA) binding free energy calculations indicated that the polar solvation free energy (ΔGpolar) of the charged peptides (LAPYK, LAPYE) were unfavorable for binding to ACE. On the other hand, the results of isothermal titration calorimetry analyses suggested that the enthalpy-driven ACE-peptide interactions were more favorable than the entropy-driven ACE-peptide interaction counterparts. |
| format | Article |
| id | doaj-art-d37bf356a4fb41db9f31af5d57c7fc22 |
| institution | Kabale University |
| issn | 2213-4530 |
| language | English |
| publishDate | 2022-11-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-d37bf356a4fb41db9f31af5d57c7fc222025-02-02T23:24:44ZengTsinghua University PressFood Science and Human Wellness2213-45302022-11-0111616231630Structural requirements and interaction mechanisms of ACE inhibitory peptides: molecular simulation and thermodynamics studies on LAPYK and its modified peptidesBiying Zhang0Jingbo Liu1Hedi Wen2Feng Jiang3Erlei Wang4Ting Zhang5Jilin Provincial Key Laboratory of Nutrition and Functional Food, College of Food Science and Engineering, Jilin University, Changchun 130062, China; College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, ChinaJilin Provincial Key Laboratory of Nutrition and Functional Food, College of Food Science and Engineering, Jilin University, Changchun 130062, ChinaJilin Provincial Key Laboratory of Nutrition and Functional Food, College of Food Science and Engineering, Jilin University, Changchun 130062, ChinaJilin Provincial Key Laboratory of Nutrition and Functional Food, College of Food Science and Engineering, Jilin University, Changchun 130062, ChinaJilin Provincial Key Laboratory of Nutrition and Functional Food, College of Food Science and Engineering, Jilin University, Changchun 130062, ChinaJilin Provincial Key Laboratory of Nutrition and Functional Food, College of Food Science and Engineering, Jilin University, Changchun 130062, China; Corresponding author.The understanding of the structural requirements and the intermolecular-interaction mechanism are important for discovering potent angiotensin-converting enzyme (ACE) inhibitory peptides. In this study, we modified an egg-white derived peptide, LAPYK, using the amino acids with different properties to produce the LAPYK-modified peptides. The ACE inhibitory activities of the modified peptides were determined to explore the structural requirements of ACE inhibitory peptides (ACEIPs). Molecular simulation and isothermal titration calorimetry analysis were used to investigate interactions between the peptides and ACE. We found that hydrophobicity and the amino acids with ring structures were beneficial for the ACE inhibitory activities of the peptides. The results of the molecular mechanics poisson boltzmann surface area (MMPBSA) binding free energy calculations indicated that the polar solvation free energy (ΔGpolar) of the charged peptides (LAPYK, LAPYE) were unfavorable for binding to ACE. On the other hand, the results of isothermal titration calorimetry analyses suggested that the enthalpy-driven ACE-peptide interactions were more favorable than the entropy-driven ACE-peptide interaction counterparts.http://www.sciencedirect.com/science/article/pii/S2213453022001045ACE inhibitory peptidesMolecular dockingMolecular dynamics simulationIsothermal titration calorimetry |
| spellingShingle | Biying Zhang Jingbo Liu Hedi Wen Feng Jiang Erlei Wang Ting Zhang Structural requirements and interaction mechanisms of ACE inhibitory peptides: molecular simulation and thermodynamics studies on LAPYK and its modified peptides Food Science and Human Wellness ACE inhibitory peptides Molecular docking Molecular dynamics simulation Isothermal titration calorimetry |
| title | Structural requirements and interaction mechanisms of ACE inhibitory peptides: molecular simulation and thermodynamics studies on LAPYK and its modified peptides |
| title_full | Structural requirements and interaction mechanisms of ACE inhibitory peptides: molecular simulation and thermodynamics studies on LAPYK and its modified peptides |
| title_fullStr | Structural requirements and interaction mechanisms of ACE inhibitory peptides: molecular simulation and thermodynamics studies on LAPYK and its modified peptides |
| title_full_unstemmed | Structural requirements and interaction mechanisms of ACE inhibitory peptides: molecular simulation and thermodynamics studies on LAPYK and its modified peptides |
| title_short | Structural requirements and interaction mechanisms of ACE inhibitory peptides: molecular simulation and thermodynamics studies on LAPYK and its modified peptides |
| title_sort | structural requirements and interaction mechanisms of ace inhibitory peptides molecular simulation and thermodynamics studies on lapyk and its modified peptides |
| topic | ACE inhibitory peptides Molecular docking Molecular dynamics simulation Isothermal titration calorimetry |
| url | http://www.sciencedirect.com/science/article/pii/S2213453022001045 |
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