O-alkylated quercetins with selective acetylcholinesterase and β-secretase inhibitions from Melicope glabra leaves, and their flavonols profile by LC-ESI-Q-TOF/MS
Intensive investigation of phytochemicals from edible Melicope glabra leaves provided a series of O-alkylated quercetins (1–13). The quercetin 1 bearing prenyl and methyl motif showed potent inhibition to human acetylcholinesterase (hAChE) with mixed type I mode, while quercetin was inactive. The po...
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| Format: | Article |
| Language: | English |
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Elsevier
2021-09-01
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| Series: | Journal of Functional Foods |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S1756464621002516 |
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| author | Aizhamal Baiseitova Abdul Bari Shah Jeong Yoon Kim Yeong Jun Ban Jeong Ho Kim Mohd Azlan Nafiah Ki Hun Park |
| author_facet | Aizhamal Baiseitova Abdul Bari Shah Jeong Yoon Kim Yeong Jun Ban Jeong Ho Kim Mohd Azlan Nafiah Ki Hun Park |
| author_sort | Aizhamal Baiseitova |
| collection | DOAJ |
| description | Intensive investigation of phytochemicals from edible Melicope glabra leaves provided a series of O-alkylated quercetins (1–13). The quercetin 1 bearing prenyl and methyl motif showed potent inhibition to human acetylcholinesterase (hAChE) with mixed type I mode, while quercetin was inactive. The position of methyl group was also a critical factor to hAChE inhibition: 1 (4′-O-methyl, IC50 = 12.7 μM) vs 2 (3′-O-methyl, IC50 = 119 μM). Inhibitory potency was doubly confirmed with the binding affinity (KSV) based on fluorescence quenching. O-Methyl groups on quercetin were observed to influence β-secretase (BACE1) inhibition. Thus, O-methylated quercetins (4–6) displayed potential inhibitions against BACE1 with IC50 values of 1.3, 4.1, and 14.1 μM, respectively. All compounds (3–6) have noncompetitive mode to BACE1. Additionally, all quercetin derivatives (1–13) had antioxidant potentials against different radical sources (ABTS, ORAC and FRAP). The UPLC-ESI-Q-TOF/MS indicated that the leaves part had promising metabolites towards hAChE and BACE1 inhibitions, which are the most predominant phytochemicals. |
| first_indexed | 2024-12-17T02:18:50Z |
| format | Article |
| id | doaj.art-f05772e8cb59432da09b90ef92e88d6c |
| institution | Directory Open Access Journal |
| issn | 1756-4646 |
| language | English |
| last_indexed | 2024-12-17T02:18:50Z |
| publishDate | 2021-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Functional Foods |
| spelling | doaj.art-f05772e8cb59432da09b90ef92e88d6c2022-12-21T22:07:20ZengElsevierJournal of Functional Foods1756-46462021-09-0184104602O-alkylated quercetins with selective acetylcholinesterase and β-secretase inhibitions from Melicope glabra leaves, and their flavonols profile by LC-ESI-Q-TOF/MSAizhamal Baiseitova0Abdul Bari Shah1Jeong Yoon Kim2Yeong Jun Ban3Jeong Ho Kim4Mohd Azlan Nafiah5Ki Hun Park6Division of Applied Life Science (BK21 plus), IALS, Gyeongsang National University, Jinju 52828, Republic of KoreaDivision of Applied Life Science (BK21 plus), IALS, Gyeongsang National University, Jinju 52828, Republic of KoreaDepartment of Pharmaceutical Engineering, IALS, Gyeongsang National University, Jinju, Republic of KoreaDivision of Applied Life Science (BK21 plus), IALS, Gyeongsang National University, Jinju 52828, Republic of KoreaDivision of Applied Life Science (BK21 plus), IALS, Gyeongsang National University, Jinju 52828, Republic of KoreaDepartment of Chemistry, Faculty of Science and Mathematics, Universiti Pendidikan Sultan Idris, 35900 Tg. Malim, Perak, MalaysiaDivision of Applied Life Science (BK21 plus), IALS, Gyeongsang National University, Jinju 52828, Republic of Korea; Corresponding author at: Division of Applied Life Science (BK21 plus), IALS, Gyeongsang National University, Jinju 52828, Republic of Korea.Intensive investigation of phytochemicals from edible Melicope glabra leaves provided a series of O-alkylated quercetins (1–13). The quercetin 1 bearing prenyl and methyl motif showed potent inhibition to human acetylcholinesterase (hAChE) with mixed type I mode, while quercetin was inactive. The position of methyl group was also a critical factor to hAChE inhibition: 1 (4′-O-methyl, IC50 = 12.7 μM) vs 2 (3′-O-methyl, IC50 = 119 μM). Inhibitory potency was doubly confirmed with the binding affinity (KSV) based on fluorescence quenching. O-Methyl groups on quercetin were observed to influence β-secretase (BACE1) inhibition. Thus, O-methylated quercetins (4–6) displayed potential inhibitions against BACE1 with IC50 values of 1.3, 4.1, and 14.1 μM, respectively. All compounds (3–6) have noncompetitive mode to BACE1. Additionally, all quercetin derivatives (1–13) had antioxidant potentials against different radical sources (ABTS, ORAC and FRAP). The UPLC-ESI-Q-TOF/MS indicated that the leaves part had promising metabolites towards hAChE and BACE1 inhibitions, which are the most predominant phytochemicals.http://www.sciencedirect.com/science/article/pii/S1756464621002516Melicope glabraAcetylcholinesteraseβ-secretaseAntioxidantPteleifolosin CPteleifolosin E |
| spellingShingle | Aizhamal Baiseitova Abdul Bari Shah Jeong Yoon Kim Yeong Jun Ban Jeong Ho Kim Mohd Azlan Nafiah Ki Hun Park O-alkylated quercetins with selective acetylcholinesterase and β-secretase inhibitions from Melicope glabra leaves, and their flavonols profile by LC-ESI-Q-TOF/MS Journal of Functional Foods Melicope glabra Acetylcholinesterase β-secretase Antioxidant Pteleifolosin C Pteleifolosin E |
| title | O-alkylated quercetins with selective acetylcholinesterase and β-secretase inhibitions from Melicope glabra leaves, and their flavonols profile by LC-ESI-Q-TOF/MS |
| title_full | O-alkylated quercetins with selective acetylcholinesterase and β-secretase inhibitions from Melicope glabra leaves, and their flavonols profile by LC-ESI-Q-TOF/MS |
| title_fullStr | O-alkylated quercetins with selective acetylcholinesterase and β-secretase inhibitions from Melicope glabra leaves, and their flavonols profile by LC-ESI-Q-TOF/MS |
| title_full_unstemmed | O-alkylated quercetins with selective acetylcholinesterase and β-secretase inhibitions from Melicope glabra leaves, and their flavonols profile by LC-ESI-Q-TOF/MS |
| title_short | O-alkylated quercetins with selective acetylcholinesterase and β-secretase inhibitions from Melicope glabra leaves, and their flavonols profile by LC-ESI-Q-TOF/MS |
| title_sort | o alkylated quercetins with selective acetylcholinesterase and β secretase inhibitions from melicope glabra leaves and their flavonols profile by lc esi q tof ms |
| topic | Melicope glabra Acetylcholinesterase β-secretase Antioxidant Pteleifolosin C Pteleifolosin E |
| url | http://www.sciencedirect.com/science/article/pii/S1756464621002516 |
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