Isoquinoline alkaloids reduce beta-amyloid peptide toxicity in Caenorhabditis elegans
| Autor: | Euzébio Guimarães Barbosa, Fernando Hallwass, Warley de Souza Borges, Estela Mariana, Daisy Sotero Chacon, Riva de Paula Oliveira, Jean Paulo de Andrade, José Angelo S. Zuanazzi, Leandro de Santis Ferreira, Thais Guaratini, Wamberto Alristenio Moreira de Almeida, Cecília Rodrigues Lucas, Raquel Brandt Giordani |
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| Rok vydání: | 2020 |
| Předmět: |
chemistry.chemical_classification
Amyloid biology Organic Chemistry Central nervous system Peptide Plant Science Pharmacology biology.organism_classification Biochemistry Analytical Chemistry chemistry.chemical_compound medicine.anatomical_structure chemistry Toxicity medicine heterocyclic compounds Isoquinoline Beta (finance) Caenorhabditis elegans |
| DOI: | 10.6084/m9.figshare.11864892.v1 |
| Popis: | Alzheimer’s disease (AD) is a multifactorial health problem widespread over the world. Regarding the historical importance of the alkaloids in the central nervous system pharmacology they remain as promising drug candidates against AD. Seven alkaloids from Amaryllidaceae and Fabaceae were evaluated in vivo, in vitro and in silico targets related to the AD pathophysiology. Erythraline and erysodine showed the greatest potential compared to Memantine, a drug currently used in AD therapy, by delaying the Aβ1-42-induced paralysis in the transgenic strain CL2006 Caenorhabditis elegans, an alternative model to assess the impairment of beta-amyloid peptide deposition. The in vitro inhibition of the acetylcholinesterase was observed for the first time for Erythrina alkaloids; however Lycorine was the most active. Docking simulation contributed to comprehend this potential by showing a hydrophobic interaction between acetylcholinesterase and Lycorine in the amino acid residue TRP 84 as well as hydrogen bonds with TRY 121 and ASP 72. |
| Databáze: | OpenAIRE |
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