Butyrylcholinesterase inhibitory activity of peptides identified from yellow field pea (Pisum sativum) enzymatic protein hydrolysates
Butyrylcholinesterase (BuChE) is an enzyme implicated in Alzheimer’s disease due to the excessive breakdown of neurotransmitters. The study screened and synthesized de novo peptides derived from yellow field pea as BuChE activity inhibitors. The conformational changes of the enzyme were evaluated to...
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| Format: | Article |
| Language: | English |
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Elsevier
2023-07-01
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| Series: | Journal of Functional Foods |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1756464623001901 |
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| author | Nancy D. Asen Ogadimma D. Okagu Chibuike C. Udenigwe Rotimi E. Aluko |
| author_facet | Nancy D. Asen Ogadimma D. Okagu Chibuike C. Udenigwe Rotimi E. Aluko |
| author_sort | Nancy D. Asen |
| collection | DOAJ |
| description | Butyrylcholinesterase (BuChE) is an enzyme implicated in Alzheimer’s disease due to the excessive breakdown of neurotransmitters. The study screened and synthesized de novo peptides derived from yellow field pea as BuChE activity inhibitors. The conformational changes of the enzyme were evaluated to confirm interaction with the peptides, along with mode of inhibition by the peptide and their binding affinity. The result showed no significant conformational changes of the enzyme after interaction with peptides. The catalytic parameters were low indicating strong affinity at low peptide concentrations and maximum velocity (Vmax) decreased with increasing peptide concentration for all the peptides. Peptides with mixed inhibition mode had low docking energy scores suggesting high affinity for BuChE and peptide-enzyme interaction were through catalytic triad and /or peripheral anionic site. Results revealed that peptides derived from yellow field pea protein could be potential inhibitors of BuChE activity and probably effective in AD therapy. |
| first_indexed | 2024-03-13T04:56:02Z |
| format | Article |
| id | doaj.art-dc3a7774d2c640318c41a451477962ad |
| institution | Directory Open Access Journal |
| issn | 1756-4646 |
| language | English |
| last_indexed | 2024-03-13T04:56:02Z |
| publishDate | 2023-07-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Functional Foods |
| spelling | doaj.art-dc3a7774d2c640318c41a451477962ad2023-06-18T05:01:20ZengElsevierJournal of Functional Foods1756-46462023-07-01106105590Butyrylcholinesterase inhibitory activity of peptides identified from yellow field pea (Pisum sativum) enzymatic protein hydrolysatesNancy D. Asen0Ogadimma D. Okagu1Chibuike C. Udenigwe2Rotimi E. Aluko3Department of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg, Manitoba R3T 2N2, CanadaDepartment of Chemistry and Biomolecular Sciences, Faculty of Science, University of Ottawa, Ottawa, ON K1N 6N5, CanadaDepartment of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada; Department of Chemistry and Biomolecular Sciences, Faculty of Science, University of Ottawa, Ottawa, ON K1N 6N5, Canada; School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, Ottawa, ON K1H 8M5, CanadaDepartment of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada; Richardson Centre for Food Technology and Research, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada; Corresponding author at: Department of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada.Butyrylcholinesterase (BuChE) is an enzyme implicated in Alzheimer’s disease due to the excessive breakdown of neurotransmitters. The study screened and synthesized de novo peptides derived from yellow field pea as BuChE activity inhibitors. The conformational changes of the enzyme were evaluated to confirm interaction with the peptides, along with mode of inhibition by the peptide and their binding affinity. The result showed no significant conformational changes of the enzyme after interaction with peptides. The catalytic parameters were low indicating strong affinity at low peptide concentrations and maximum velocity (Vmax) decreased with increasing peptide concentration for all the peptides. Peptides with mixed inhibition mode had low docking energy scores suggesting high affinity for BuChE and peptide-enzyme interaction were through catalytic triad and /or peripheral anionic site. Results revealed that peptides derived from yellow field pea protein could be potential inhibitors of BuChE activity and probably effective in AD therapy.http://www.sciencedirect.com/science/article/pii/S1756464623001901ButyrylcholinesterasePeptideInhibitionKineticsMolecular dockingAlzheimer’s disease |
| spellingShingle | Nancy D. Asen Ogadimma D. Okagu Chibuike C. Udenigwe Rotimi E. Aluko Butyrylcholinesterase inhibitory activity of peptides identified from yellow field pea (Pisum sativum) enzymatic protein hydrolysates Journal of Functional Foods Butyrylcholinesterase Peptide Inhibition Kinetics Molecular docking Alzheimer’s disease |
| title | Butyrylcholinesterase inhibitory activity of peptides identified from yellow field pea (Pisum sativum) enzymatic protein hydrolysates |
| title_full | Butyrylcholinesterase inhibitory activity of peptides identified from yellow field pea (Pisum sativum) enzymatic protein hydrolysates |
| title_fullStr | Butyrylcholinesterase inhibitory activity of peptides identified from yellow field pea (Pisum sativum) enzymatic protein hydrolysates |
| title_full_unstemmed | Butyrylcholinesterase inhibitory activity of peptides identified from yellow field pea (Pisum sativum) enzymatic protein hydrolysates |
| title_short | Butyrylcholinesterase inhibitory activity of peptides identified from yellow field pea (Pisum sativum) enzymatic protein hydrolysates |
| title_sort | butyrylcholinesterase inhibitory activity of peptides identified from yellow field pea pisum sativum enzymatic protein hydrolysates |
| topic | Butyrylcholinesterase Peptide Inhibition Kinetics Molecular docking Alzheimer’s disease |
| url | http://www.sciencedirect.com/science/article/pii/S1756464623001901 |
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