In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase
Zephyranthes carinata Herb., a specie of the Amaryllidoideae subfamily, has been reported to have inhibitory activity against acetylcholinesterase. However, scientific evidence related to their bioactive alkaloids has been lacking. Thus, this study describes the isolation of the alkaloids of this pl...
- Autores:
-
Sierra, Karina
De Andrade, Jean Paulo
Angel Villalba, Javier R
Osorio, Edison
Yañéz, Osvaldo
Guaita Martínez, José Manuel
Oleas, Nora H.
García-Beltrán, Olimpo
De S. Borges, Warley
Bastida, Jaume
Osorio, Edison
Cortes, Natalie
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2022
- Institución:
- Universidad de Ibagué
- Repositorio:
- Repositorio Universidad de Ibagué
- Idioma:
- eng
- OAI Identifier:
- oai:repositorio.unibague.edu.co:20.500.12313/5488
- Acceso en línea:
- https://www.sciencedirect.com/science/article/pii/S075333222200405X
- Palabra clave:
- Alcaloides de Amaryllidaceae Galantina
Acetylcholinesterase inhibition
Amaryllidaceae alkaloids
Galanthine; Molecular docking
Molecular dynamics
- Rights
- openAccess
- License
- http://purl.org/coar/access_right/c_abf2
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| dc.title.eng.fl_str_mv |
In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase |
| title |
In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase |
| spellingShingle |
In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase Alcaloides de Amaryllidaceae Galantina Acetylcholinesterase inhibition Amaryllidaceae alkaloids Galanthine; Molecular docking Molecular dynamics |
| title_short |
In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase |
| title_full |
In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase |
| title_fullStr |
In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase |
| title_full_unstemmed |
In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase |
| title_sort |
In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase |
| dc.creator.fl_str_mv |
Sierra, Karina De Andrade, Jean Paulo Angel Villalba, Javier R Osorio, Edison Yañéz, Osvaldo Guaita Martínez, José Manuel Oleas, Nora H. García-Beltrán, Olimpo De S. Borges, Warley Bastida, Jaume Osorio, Edison Cortes, Natalie |
| dc.contributor.author.none.fl_str_mv |
Sierra, Karina De Andrade, Jean Paulo Angel Villalba, Javier R Osorio, Edison Yañéz, Osvaldo Guaita Martínez, José Manuel Oleas, Nora H. García-Beltrán, Olimpo De S. Borges, Warley Bastida, Jaume Osorio, Edison Cortes, Natalie |
| dc.subject.armarc.none.fl_str_mv |
Alcaloides de Amaryllidaceae Galantina |
| topic |
Alcaloides de Amaryllidaceae Galantina Acetylcholinesterase inhibition Amaryllidaceae alkaloids Galanthine; Molecular docking Molecular dynamics |
| dc.subject.proposal.eng.fl_str_mv |
Acetylcholinesterase inhibition Amaryllidaceae alkaloids Galanthine; Molecular docking Molecular dynamics |
| description |
Zephyranthes carinata Herb., a specie of the Amaryllidoideae subfamily, has been reported to have inhibitory activity against acetylcholinesterase. However, scientific evidence related to their bioactive alkaloids has been lacking. Thus, this study describes the isolation of the alkaloids of this plant, and their inhibition of the enzymes acetylcholinesterase (eeAChE) and butyrylcholinesterase (eqBuChE), being galanthine the main component. Additionally, haemanthamine, hamayne, lycoramine, lycorine, tazettine, trisphaeridine and vittatine/crinine were also isolated. The results showed that galanthine has significant activity at low micromolar concentrations for eeAChE (IC50 = 1.96 μg/mL). The in-silico study allowed to establish at a molecular level the high affinity and the way galanthine interacts with the active site of the TcAChE enzyme, information that corroborates the result of the experimental IC50. However, according to molecular dynamics (MD) analysis, it is also suggested that galanthine presents a different inhibition mode that the one observed for galanthamine, by presenting interaction with peripheral anionic binding site of the enzyme, which prevents the entrance and exit of molecules from the active site. Thus, in vitro screening assays plus rapid computer development play an essential role in the search for new cholinesterase inhibitors by identifying unknown bio-interactions between bioactive compounds and biological targets. © 2022 The Authors |
| publishDate |
2022 |
| dc.date.issued.none.fl_str_mv |
2022 |
| dc.date.accessioned.none.fl_str_mv |
2025-08-15T20:00:39Z |
| dc.date.available.none.fl_str_mv |
2025-08-15T20:00:39Z |
| dc.type.none.fl_str_mv |
Artículo de revista |
| dc.type.coar.none.fl_str_mv |
http://purl.org/coar/resource_type/c_2df8fbb1 |
| dc.type.coarversion.none.fl_str_mv |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| dc.type.content.none.fl_str_mv |
Text |
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info:eu-repo/semantics/article |
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info:eu-repo/semantics/publishedVersion |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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publishedVersion |
| dc.identifier.citation.none.fl_str_mv |
Sierra, K., de Andrade, J., R. Tallini, L., Osorio, E., Yañéz, O., Osorio, M., Oleas, N., García-Beltrán, O., de S. Borges, W., Bastida, J., Osorio, E y Osorio, E. (2022). In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase. Biomedicine and Pharmacotherap, 150. DOI: 10.1016/j.biopha.2022.113016 |
| dc.identifier.doi.none.fl_str_mv |
10.1016/j.biopha.2022.113016 |
| dc.identifier.eissn.none.fl_str_mv |
19506007 |
| dc.identifier.issn.none.fl_str_mv |
07533322 |
| dc.identifier.uri.none.fl_str_mv |
|
| dc.identifier.url.none.fl_str_mv |
https://www.sciencedirect.com/science/article/pii/S075333222200405X |
| identifier_str_mv |
Sierra, K., de Andrade, J., R. Tallini, L., Osorio, E., Yañéz, O., Osorio, M., Oleas, N., García-Beltrán, O., de S. Borges, W., Bastida, J., Osorio, E y Osorio, E. (2022). In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase. Biomedicine and Pharmacotherap, 150. DOI: 10.1016/j.biopha.2022.113016 10.1016/j.biopha.2022.113016 19506007 07533322 |
| url |
https://www.sciencedirect.com/science/article/pii/S075333222200405X |
| dc.language.iso.none.fl_str_mv |
eng |
| language |
eng |
| dc.relation.citationstartpage.none.fl_str_mv |
113016 |
| dc.relation.citationvolume.none.fl_str_mv |
150 |
| dc.relation.ispartofjournal.none.fl_str_mv |
Biomedicine and Pharmacotherapy |
| dc.relation.references.none.fl_str_mv |
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Sierra, Karina0d72ff29-5bb7-4723-9a22-ae2f0cb6ecbd-1De Andrade, Jean Paulo4348cbf9-fe36-457c-8665-daf47d388a4b-1Angel Villalba, Javier R800083c9-9860-410a-8c45-03ba4825d091600Osorio, Edisone6d834e4-46ca-40f0-ab7c-630a35856901-1Yañéz, Osvaldo1e46de30-fe40-4d34-8d2d-6f1f3a94d019-1Guaita Martínez, José Manuelb1241368-59c4-4cf5-ab02-bc5bc39fab98600Oleas, Nora H.e2053042-c304-40be-b616-3c40f83c279c-1García-Beltrán, Olimpodfe2bbe7-81d5-415c-9be6-6469a5a40c75-1De S. Borges, Warley70b8ce74-e6b9-46e3-9a4b-1498f3638f55-1Bastida, Jaume00ea29d6-11a2-48bd-bc9e-2dd48a2bc06e-1Osorio, Edisone6d834e4-46ca-40f0-ab7c-630a35856901-1Cortes, Nataliece9c654f-72b9-4163-a73a-c1c71903ba7e-12025-08-15T20:00:39Z2025-08-15T20:00:39Z2022Zephyranthes carinata Herb., a specie of the Amaryllidoideae subfamily, has been reported to have inhibitory activity against acetylcholinesterase. However, scientific evidence related to their bioactive alkaloids has been lacking. Thus, this study describes the isolation of the alkaloids of this plant, and their inhibition of the enzymes acetylcholinesterase (eeAChE) and butyrylcholinesterase (eqBuChE), being galanthine the main component. Additionally, haemanthamine, hamayne, lycoramine, lycorine, tazettine, trisphaeridine and vittatine/crinine were also isolated. The results showed that galanthine has significant activity at low micromolar concentrations for eeAChE (IC50 = 1.96 μg/mL). The in-silico study allowed to establish at a molecular level the high affinity and the way galanthine interacts with the active site of the TcAChE enzyme, information that corroborates the result of the experimental IC50. However, according to molecular dynamics (MD) analysis, it is also suggested that galanthine presents a different inhibition mode that the one observed for galanthamine, by presenting interaction with peripheral anionic binding site of the enzyme, which prevents the entrance and exit of molecules from the active site. Thus, in vitro screening assays plus rapid computer development play an essential role in the search for new cholinesterase inhibitors by identifying unknown bio-interactions between bioactive compounds and biological targets. © 2022 The Authorsapplication/pdfSierra, K., de Andrade, J., R. Tallini, L., Osorio, E., Yañéz, O., Osorio, M., Oleas, N., García-Beltrán, O., de S. Borges, W., Bastida, J., Osorio, E y Osorio, E. (2022). In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase. Biomedicine and Pharmacotherap, 150. DOI: 10.1016/j.biopha.2022.11301610.1016/j.biopha.2022.1130161950600707533322https://www.sciencedirect.com/science/article/pii/S075333222200405XengElsevier Masson S.R.L.France113016150Biomedicine and PharmacotherapyWorld Health Organization (WHO), The top 10 causes of death, (2018). https://www.who.int/news-room/fact-sheets/detail/the-top-10-causes-of-death (accessed July 24, 2020).A. Association 2019 Alzheimer’s disease facts and figures Alzheimer’s Dement, 15 (2019), pp. 321-387, 10.1016/j.jalz.2019.01.010A.A.D.T. Abeysinghe, R.D.U.S. Deshapriya, C. Udawatte Alzheimer’s disease; a review of the pathophysiological basis and therapeutic interventions Life Sci., 256 (2020), Article 117996, 10.1016/j.lfs.2020.117996Ł.J. Walczak-Nowicka, M. Herbet Acetylcholinesterase inhibitors in the treatment of neurodegenerative diseases and the role of acetylcholinesterase in their pathogenesis 2021, Vol. 22, Page 9290 Int. J. Mol. Sci., 22 (2021), p. 9290, 10.3390/IJMS22179290R. Hussain, H. 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Trujillo-Ferrara, R. Miranda, C.A. Flores-Sandoval QSAR, docking, dynamic simulation and quantum mechanics studies to explore the recognition properties of cholinesterase binding sites Chem. Biol. Interact., 209 (2014), pp. 1-13, 10.1016/j.cbi.2013.12.001I. Silman, J.L. Sussman Acetylcholinesterase: how is structure related to function? Chem. Biol. Interact., 175 (2008), pp. 3-10, 10.1016/J.CBI.2008.05.035Copyright © 2025 Elsevier B.V., its licensors, and contributors. All rights are reserved, including those for text and data mining, AI training, and similar technologies. For all open access content, the relevant licensing terms apply.info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Atribución-NoComercial 4.0 Internacional (CC BY-NC 4.0)https://creativecommons.org/licenses/by-nc/4.0/https://www.sciencedirect.com/science/article/pii/S075333222200405XAlcaloides de Amaryllidaceae GalantinaAcetylcholinesterase inhibitionAmaryllidaceae alkaloidsGalanthine; Molecular dockingMolecular dynamicsIn vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesteraseArtículo de revistahttp://purl.org/coar/resource_type/c_2df8fbb1http://purl.org/coar/version/c_970fb48d4fbd8a85Textinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionPublicationTEXTArtículo.pdf.txtArtículo.pdf.txtExtracted texttext/plain5043https://repositorio.unibague.edu.co/bitstreams/633a056d-1b75-4811-8244-2f40fcb2b79f/downloaddbb5086e29a80cf4aeedb23313f40dd9MD53THUMBNAILArtículo.pdf.jpgArtículo.pdf.jpgIM Thumbnailimage/jpeg28231https://repositorio.unibague.edu.co/bitstreams/78dad178-9614-4bff-84f8-806b555e7a70/download2f7a941f98c10c6ced5119fd94276b6fMD54LICENSElicense.txtlicense.txttext/plain; charset=utf-8134https://repositorio.unibague.edu.co/bitstreams/7970ac01-b5b5-413f-b916-8a601b0f817d/download2fa3e590786b9c0f3ceba1b9656b7ac3MD51ORIGINALArtículo.pdfArtículo.pdfapplication/pdf271629https://repositorio.unibague.edu.co/bitstreams/6d3374af-a4ea-4955-b167-598e1afe584d/downloadeb01686f1376e5fab680b687ff331028MD5220.500.12313/5488oai:repositorio.unibague.edu.co:20.500.12313/54882025-09-12 10:56:01.128https://creativecommons.org/licenses/by-nc/4.0/Copyright © 2025 Elsevier B.V., its licensors, and contributors. All rights are reserved, including those for text and data mining, AI training, and similar technologies. For all open access content, the relevant licensing terms apply.https://repositorio.unibague.edu.coRepositorio Institucional Universidad de Ibaguébdigital@metabiblioteca.comQ3JlYXRpdmUgQ29tbW9ucyBBdHRyaWJ1dGlvbi1Ob25Db21tZXJjaWFsLU5vRGVyaXZhdGl2ZXMgNC4wIEludGVybmF0aW9uYWwgTGljZW5zZQ0KaHR0cHM6Ly9jcmVhdGl2ZWNvbW1vbnMub3JnL2xpY2Vuc2VzL2J5LW5jLW5kLzQuMC8= |