Enzyme kinetics, molecular docking, and in silico characterization of canary seed (Phalaris canariensis L.) peptides with ACE and pancreatic lipase inhibitory activity
The bioactivity of canary seed peptides (CSP) towards metabolism-regulating enzymes was evaluated. Peptides with angiotensin-converting enzyme (ACE), dipeptidyl peptidase IV (DPP-IV), and pancreatic lipase activity remained stable (p < 0.05) to simulated gastrointestinal digestion (SGD). CSP-SGD...
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| Format: | Article |
| Language: | English |
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Elsevier
2022-01-01
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| Series: | Journal of Functional Foods |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S1756464621005417 |
| _version_ | 1819172234117251072 |
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| author | Uriel Urbizo-Reyes Andrea M. Liceaga Lavanya Reddivari Kee-Hong Kim Joseph M. Anderson |
| author_facet | Uriel Urbizo-Reyes Andrea M. Liceaga Lavanya Reddivari Kee-Hong Kim Joseph M. Anderson |
| author_sort | Uriel Urbizo-Reyes |
| collection | DOAJ |
| description | The bioactivity of canary seed peptides (CSP) towards metabolism-regulating enzymes was evaluated. Peptides with angiotensin-converting enzyme (ACE), dipeptidyl peptidase IV (DPP-IV), and pancreatic lipase activity remained stable (p < 0.05) to simulated gastrointestinal digestion (SGD). CSP-SGD were transported efficiently (>10%) through the Caco-2 monolayer, indicating absorption through the intestinal epithelium. Lineweaver-Burk plots demonstrated that CSP-SGD act as mixed-type inhibitors for DPP-IV and α-glucosidase. Furthermore, CSP-SGD were potent as antihypertensive and antiobesity agents. Molecular docking and in silico analyses were targeted to understand CSP-SGD interactions with ACE and pancreatic lipase. ACE-inhibitory peptides (LHPQ, QTPHQ, KPVPR, and ELHPQ) acted as non-competitive inhibitors by destabilization of the transition state and Zn(II) coordination in ACE. The uncompetitive inhibition of pancreatic lipase by peptides (VPPR, LADR, LSPR, and TVGPR) destabilized the open-lid conformation of pancreatic lipase. The results of this study showed that canary seed proteins could serve as a source of biologically active peptides. |
| first_indexed | 2024-12-22T20:03:56Z |
| format | Article |
| id | doaj.art-86d823cd3d804e0ca49add5faab370f8 |
| institution | Directory Open Access Journal |
| issn | 1756-4646 |
| language | English |
| last_indexed | 2024-12-22T20:03:56Z |
| publishDate | 2022-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Functional Foods |
| spelling | doaj.art-86d823cd3d804e0ca49add5faab370f82022-12-21T18:14:11ZengElsevierJournal of Functional Foods1756-46462022-01-0188104892Enzyme kinetics, molecular docking, and in silico characterization of canary seed (Phalaris canariensis L.) peptides with ACE and pancreatic lipase inhibitory activityUriel Urbizo-Reyes0Andrea M. Liceaga1Lavanya Reddivari2Kee-Hong Kim3Joseph M. Anderson4Protein Chemistry and Bioactive Peptides Laboratory, Purdue University, 745 Agriculture Mall Drive, West Lafayette, IN 47907, USA; Department of Food Science, Purdue University, 745 Agriculture Mall Drive, West Lafayette, IN 47907, USAProtein Chemistry and Bioactive Peptides Laboratory, Purdue University, 745 Agriculture Mall Drive, West Lafayette, IN 47907, USA; Department of Food Science, Purdue University, 745 Agriculture Mall Drive, West Lafayette, IN 47907, USA; Corresponding author at: Protein Chemistry and Bioactive Peptides Laboratory, Purdue University, 745 Agriculture Mall Drive, West Lafayette, IN 47907, USA.Department of Food Science, Purdue University, 745 Agriculture Mall Drive, West Lafayette, IN 47907, USADepartment of Food Science, Purdue University, 745 Agriculture Mall Drive, West Lafayette, IN 47907, USAUSDA-ARS, Department of Agronomy, Purdue University, 915 W. State St., West Lafayette, IN 47907, USAThe bioactivity of canary seed peptides (CSP) towards metabolism-regulating enzymes was evaluated. Peptides with angiotensin-converting enzyme (ACE), dipeptidyl peptidase IV (DPP-IV), and pancreatic lipase activity remained stable (p < 0.05) to simulated gastrointestinal digestion (SGD). CSP-SGD were transported efficiently (>10%) through the Caco-2 monolayer, indicating absorption through the intestinal epithelium. Lineweaver-Burk plots demonstrated that CSP-SGD act as mixed-type inhibitors for DPP-IV and α-glucosidase. Furthermore, CSP-SGD were potent as antihypertensive and antiobesity agents. Molecular docking and in silico analyses were targeted to understand CSP-SGD interactions with ACE and pancreatic lipase. ACE-inhibitory peptides (LHPQ, QTPHQ, KPVPR, and ELHPQ) acted as non-competitive inhibitors by destabilization of the transition state and Zn(II) coordination in ACE. The uncompetitive inhibition of pancreatic lipase by peptides (VPPR, LADR, LSPR, and TVGPR) destabilized the open-lid conformation of pancreatic lipase. The results of this study showed that canary seed proteins could serve as a source of biologically active peptides.http://www.sciencedirect.com/science/article/pii/S1756464621005417Canary seedBiopeptidesMolecular dockingPancreatic lipaseAngiotensin converting enzyme |
| spellingShingle | Uriel Urbizo-Reyes Andrea M. Liceaga Lavanya Reddivari Kee-Hong Kim Joseph M. Anderson Enzyme kinetics, molecular docking, and in silico characterization of canary seed (Phalaris canariensis L.) peptides with ACE and pancreatic lipase inhibitory activity Journal of Functional Foods Canary seed Biopeptides Molecular docking Pancreatic lipase Angiotensin converting enzyme |
| title | Enzyme kinetics, molecular docking, and in silico characterization of canary seed (Phalaris canariensis L.) peptides with ACE and pancreatic lipase inhibitory activity |
| title_full | Enzyme kinetics, molecular docking, and in silico characterization of canary seed (Phalaris canariensis L.) peptides with ACE and pancreatic lipase inhibitory activity |
| title_fullStr | Enzyme kinetics, molecular docking, and in silico characterization of canary seed (Phalaris canariensis L.) peptides with ACE and pancreatic lipase inhibitory activity |
| title_full_unstemmed | Enzyme kinetics, molecular docking, and in silico characterization of canary seed (Phalaris canariensis L.) peptides with ACE and pancreatic lipase inhibitory activity |
| title_short | Enzyme kinetics, molecular docking, and in silico characterization of canary seed (Phalaris canariensis L.) peptides with ACE and pancreatic lipase inhibitory activity |
| title_sort | enzyme kinetics molecular docking and in silico characterization of canary seed phalaris canariensis l peptides with ace and pancreatic lipase inhibitory activity |
| topic | Canary seed Biopeptides Molecular docking Pancreatic lipase Angiotensin converting enzyme |
| url | http://www.sciencedirect.com/science/article/pii/S1756464621005417 |
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