Identification and molecular mechanism of angiotensin-converting enzyme inhibitory peptides from Larimichthys crocea titin
This study aimed to identify novel ACEI peptides from Larimichthys crocea titin using in silico approaches and to clarify the molecular interaction mechanism. The hydrolyzed peptides of titin were compared with known ACEI peptides in the AHTPDB and BIOPEP-UWM database. Furthermore, peptides were eva...
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| Format: | Article |
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Tsinghua University Press
2020-09-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453020301294 |
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| author | Yue Fan Zhipeng Yu Wenzhu Zhao Long Ding Fuping Zheng Jianrong Li Jingbo Liu |
| author_facet | Yue Fan Zhipeng Yu Wenzhu Zhao Long Ding Fuping Zheng Jianrong Li Jingbo Liu |
| author_sort | Yue Fan |
| collection | DOAJ |
| description | This study aimed to identify novel ACEI peptides from Larimichthys crocea titin using in silico approaches and to clarify the molecular interaction mechanism. The hydrolyzed peptides of titin were compared with known ACEI peptides in the AHTPDB and BIOPEP-UWM database. Furthermore, peptides were evaluated for their solubility, ADMET properties, △G (kcal/mol) values, and in vitro ACEI activity. Molecular mechanism of ACE-peptide was performed by molecular interactions and binding orientation study. The results revealed that IC50 values of Trp-Ala-Arg(WAR) and Trp-Gln-Arg(WQR) were (31.2 ± 0.8) and (231.33 ± 0.02) μmol/L, respectively. The docking interactions result suggested that ACE-WAR and ACE-WQR complexes have same binding site, including the residues LYS511, TYR520, TYR523, HIS353, and HIS513. Molecular docking of two tripeptides WAR and WQR with ACE studies predicted their binding site and clarified the interaction between ACE and its inhibitors. The molecular docking data are consistent with the ACE inhibitory activity of the studied peptides. The results showed that Larimichthys crocea titin may be a valuable source for developing nutraceutical food. |
| format | Article |
| id | doaj-art-47e3eb673c52401da6271c4b89499623 |
| institution | Kabale University |
| issn | 2213-4530 |
| language | English |
| publishDate | 2020-09-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-47e3eb673c52401da6271c4b894996232025-02-03T10:32:33ZengTsinghua University PressFood Science and Human Wellness2213-45302020-09-0193257263Identification and molecular mechanism of angiotensin-converting enzyme inhibitory peptides from Larimichthys crocea titinYue Fan0Zhipeng Yu1Wenzhu Zhao2Long Ding3Fuping Zheng4Jianrong Li5Jingbo Liu6College of Food Science and Engineering, Bohai University, Jinzhou, 121013, ChinaCollege of Food Science and Engineering, Bohai University, Jinzhou, 121013, China; Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University (BTBU), Beijing, 102488, China; Corresponding author at: Jinzhou, Liaoning, PR China.College of Food Science and Engineering, Bohai University, Jinzhou, 121013, ChinaCollege of Food Science and Engineering, Northwest A&F University, Yangling, 712100, ChinaBeijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University (BTBU), Beijing, 102488, ChinaBeijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University (BTBU), Beijing, 102488, ChinaLab of Nutrition and Functional Food, Jilin University, Changchun, 130062, ChinaThis study aimed to identify novel ACEI peptides from Larimichthys crocea titin using in silico approaches and to clarify the molecular interaction mechanism. The hydrolyzed peptides of titin were compared with known ACEI peptides in the AHTPDB and BIOPEP-UWM database. Furthermore, peptides were evaluated for their solubility, ADMET properties, △G (kcal/mol) values, and in vitro ACEI activity. Molecular mechanism of ACE-peptide was performed by molecular interactions and binding orientation study. The results revealed that IC50 values of Trp-Ala-Arg(WAR) and Trp-Gln-Arg(WQR) were (31.2 ± 0.8) and (231.33 ± 0.02) μmol/L, respectively. The docking interactions result suggested that ACE-WAR and ACE-WQR complexes have same binding site, including the residues LYS511, TYR520, TYR523, HIS353, and HIS513. Molecular docking of two tripeptides WAR and WQR with ACE studies predicted their binding site and clarified the interaction between ACE and its inhibitors. The molecular docking data are consistent with the ACE inhibitory activity of the studied peptides. The results showed that Larimichthys crocea titin may be a valuable source for developing nutraceutical food.http://www.sciencedirect.com/science/article/pii/S2213453020301294ACE peptideIdentificationIn silico approachesADMETMolecular docking |
| spellingShingle | Yue Fan Zhipeng Yu Wenzhu Zhao Long Ding Fuping Zheng Jianrong Li Jingbo Liu Identification and molecular mechanism of angiotensin-converting enzyme inhibitory peptides from Larimichthys crocea titin Food Science and Human Wellness ACE peptide Identification In silico approaches ADMET Molecular docking |
| title | Identification and molecular mechanism of angiotensin-converting enzyme inhibitory peptides from Larimichthys crocea titin |
| title_full | Identification and molecular mechanism of angiotensin-converting enzyme inhibitory peptides from Larimichthys crocea titin |
| title_fullStr | Identification and molecular mechanism of angiotensin-converting enzyme inhibitory peptides from Larimichthys crocea titin |
| title_full_unstemmed | Identification and molecular mechanism of angiotensin-converting enzyme inhibitory peptides from Larimichthys crocea titin |
| title_short | Identification and molecular mechanism of angiotensin-converting enzyme inhibitory peptides from Larimichthys crocea titin |
| title_sort | identification and molecular mechanism of angiotensin converting enzyme inhibitory peptides from larimichthys crocea titin |
| topic | ACE peptide Identification In silico approaches ADMET Molecular docking |
| url | http://www.sciencedirect.com/science/article/pii/S2213453020301294 |
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