Bioguided Isolation and Structure Identification of Acetylcholinesterase Enzyme Inhibitors from Drynariae Rhizome
Drynariae Rhizome, widely distributed in southern China, was clinically used as a traditional treatment for cognitive disfunction, such as Alzheimer’s disease (AD). The aim of our work was to evaluate the AChE inhibition activities of extracts of Drynariae Rhizome and pure compounds using a bioguide...
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Wiley
2020-01-01
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| Series: | Journal of Analytical Methods in Chemistry |
| Online Access: | http://dx.doi.org/10.1155/2020/2971841 |
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| author | Ming-Yang Liu Fan Zeng Yue Shen Yu-Ying Wang Ning Zhang Fang Geng |
| author_facet | Ming-Yang Liu Fan Zeng Yue Shen Yu-Ying Wang Ning Zhang Fang Geng |
| author_sort | Ming-Yang Liu |
| collection | DOAJ |
| description | Drynariae Rhizome, widely distributed in southern China, was clinically used as a traditional treatment for cognitive disfunction, such as Alzheimer’s disease (AD). The aim of our work was to evaluate the AChE inhibition activities of extracts of Drynariae Rhizome and pure compounds using a bioguided fractionation procedure. The classical approach for screening potential AChE inhibitors was developed by Ellman. However, the background color of compounds or herb extracts remained uncertain and frequently interfered with the detection of the secondary reaction, thereby easily yielding false positive or false negative results. Here, a high-throughput assay monitoring the transformation of iodized choline from iodized acetylcholine catalyzed by AChE was established based on UPLC-MS/MS. The bioguided fractionation of the extract using this method resulted in the isolation of eight AChE inhibitory flavonoids, including naringenin, eriodictyol, kaempferol, luteolin, astragalin, luteolin-7-O-β-D-glucoside, naringin, and neoeriocitrin, with the IC50 values of 3.81 ± 0.21 μM, 7.19 ± 0.62 μM, 11.09 ± 1.02 μM, 17.26 ± 0.23 μM, 18.24 ± 2.33 μM, 17.13 ± 1.02 μM, 26.4 ± 1.17 μM, and 22.49 ± 1.25 μM. It is assumed that the identified flavonoids contribute to the AChE inhibition activity of Drynariae Rhizome. These results are in agreement with the traditional uses of Drynariae Rhizome for AD. |
| format | Article |
| id | doaj-art-ef3819be9bc44a7c959cc1a06c5d52dc |
| institution | Kabale University |
| issn | 2090-8865 2090-8873 |
| language | English |
| publishDate | 2020-01-01 |
| publisher | Wiley |
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| series | Journal of Analytical Methods in Chemistry |
| spelling | doaj-art-ef3819be9bc44a7c959cc1a06c5d52dc2025-02-03T06:05:37ZengWileyJournal of Analytical Methods in Chemistry2090-88652090-88732020-01-01202010.1155/2020/29718412971841Bioguided Isolation and Structure Identification of Acetylcholinesterase Enzyme Inhibitors from Drynariae RhizomeMing-Yang Liu0Fan Zeng1Yue Shen2Yu-Ying Wang3Ning Zhang4Fang Geng5Key Laboratory of Photochemistry Biomaterials and Energy Storage Materials of Heilongjiang Province, College of Chemistry & Chemical Engineering, Harbin Normal University, Harbin 150025, ChinaKey Laboratory of Photochemistry Biomaterials and Energy Storage Materials of Heilongjiang Province, College of Chemistry & Chemical Engineering, Harbin Normal University, Harbin 150025, ChinaKey Laboratory of Photochemistry Biomaterials and Energy Storage Materials of Heilongjiang Province, College of Chemistry & Chemical Engineering, Harbin Normal University, Harbin 150025, ChinaKey Laboratory of Photochemistry Biomaterials and Energy Storage Materials of Heilongjiang Province, College of Chemistry & Chemical Engineering, Harbin Normal University, Harbin 150025, ChinaCollege of Jiamusi, Heilongjiang University of Chinese Medicine, Jiamusi, Harbin, Heilongjiang 154007, ChinaKey Laboratory of Photochemistry Biomaterials and Energy Storage Materials of Heilongjiang Province, College of Chemistry & Chemical Engineering, Harbin Normal University, Harbin 150025, ChinaDrynariae Rhizome, widely distributed in southern China, was clinically used as a traditional treatment for cognitive disfunction, such as Alzheimer’s disease (AD). The aim of our work was to evaluate the AChE inhibition activities of extracts of Drynariae Rhizome and pure compounds using a bioguided fractionation procedure. The classical approach for screening potential AChE inhibitors was developed by Ellman. However, the background color of compounds or herb extracts remained uncertain and frequently interfered with the detection of the secondary reaction, thereby easily yielding false positive or false negative results. Here, a high-throughput assay monitoring the transformation of iodized choline from iodized acetylcholine catalyzed by AChE was established based on UPLC-MS/MS. The bioguided fractionation of the extract using this method resulted in the isolation of eight AChE inhibitory flavonoids, including naringenin, eriodictyol, kaempferol, luteolin, astragalin, luteolin-7-O-β-D-glucoside, naringin, and neoeriocitrin, with the IC50 values of 3.81 ± 0.21 μM, 7.19 ± 0.62 μM, 11.09 ± 1.02 μM, 17.26 ± 0.23 μM, 18.24 ± 2.33 μM, 17.13 ± 1.02 μM, 26.4 ± 1.17 μM, and 22.49 ± 1.25 μM. It is assumed that the identified flavonoids contribute to the AChE inhibition activity of Drynariae Rhizome. These results are in agreement with the traditional uses of Drynariae Rhizome for AD.http://dx.doi.org/10.1155/2020/2971841 |
| spellingShingle | Ming-Yang Liu Fan Zeng Yue Shen Yu-Ying Wang Ning Zhang Fang Geng Bioguided Isolation and Structure Identification of Acetylcholinesterase Enzyme Inhibitors from Drynariae Rhizome Journal of Analytical Methods in Chemistry |
| title | Bioguided Isolation and Structure Identification of Acetylcholinesterase Enzyme Inhibitors from Drynariae Rhizome |
| title_full | Bioguided Isolation and Structure Identification of Acetylcholinesterase Enzyme Inhibitors from Drynariae Rhizome |
| title_fullStr | Bioguided Isolation and Structure Identification of Acetylcholinesterase Enzyme Inhibitors from Drynariae Rhizome |
| title_full_unstemmed | Bioguided Isolation and Structure Identification of Acetylcholinesterase Enzyme Inhibitors from Drynariae Rhizome |
| title_short | Bioguided Isolation and Structure Identification of Acetylcholinesterase Enzyme Inhibitors from Drynariae Rhizome |
| title_sort | bioguided isolation and structure identification of acetylcholinesterase enzyme inhibitors from drynariae rhizome |
| url | http://dx.doi.org/10.1155/2020/2971841 |
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