| Autor: |
Evelyn Muñoz-Nuñez, Soledad Quiroz-Carreño, Edgar Pastene-Navarrete, David S. Seigler, Carlos Céspedes-Acuña, Ignacio Martínez Valenzuela, Martina Oppliger Muñoz, Alexis Salas-Burgos, Julio Alarcón-Enos |
| Jazyk: |
angličtina |
| Rok vydání: |
2022 |
| Předmět: |
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| Zdroj: |
Metabolites, Vol 12, Iss 7, p 668 (2022) |
| Druh dokumentu: |
article |
| ISSN: |
2218-1989 |
| DOI: |
10.3390/metabo12070668 |
| Popis: |
The purpose of this study was to determine the inhibitory capacity of ceanothanes triterpenes isolate from Chilean Rhamnaceae on acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes. Seven ceanothanes triterpenes were isolated from aerial parts of plant material by classical phytochemical methods or prepared by the hemisynthetic method. Structures were determined by the spectroscopic method (1H-NMR and 13C NMR) and mass spectrometry (MS). AChE and BChE activity were determined by the Ellmann method for all compounds. All tested compounds exerted a greater affinity to AChE than to BChE, where compound 3 has an IC50 of 0.126 uM for AChE and of >500 uM to BChE. Kinetic studies indicated that its inhibition was competitive and reversible. According to the molecular coupling and displacement studies of the propidium iodide test, the inhibitory effect of compound 3 would be produced by interaction with the peripheral anionic site (PAS) of AChE. The compounds tested (1–7) showed an important inhibitory activity of AChE, binding to PAS. Therefore, inhibitors that bind to PAS would prevent the formation of the AChE-Aβ complex, constituting a new alternative in the treatment of Alzheimer’s disease (AD). |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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