In vitro anticholinesterase and neurotoxicity activities of Ocotea aciphylla fractions

Carneiro, Monique Marylin A de A.; Conceição, Rodrigo Souza; Reis, Isabella Mary Alves; Silva, Alessandra Bispo da; Oliveira, Joana Da Luz; Branco, Alexsandro; Costa, Sílvia Lima; Botura, Mariana Borges

doi:10.4103/pm.pm_366_17

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“…The Ocotea genus is spread in the Brazilian northeastern semiarid region and has been related to several biological activities, such as the anticholinesterase effect of its extracts, including Ocotea percoriacea (Cassiano et al, 2019) and O. aciphylla (Carneiro et al, 2018). Chemical investigations in several species of Ocotea have led to the isolation of a variety of secondary metabolites, such as alkaloids, lignans, flavonoids, and sesquiterpenes that have a remarkable economical potential, in terms of generating medicinal bioproducts, yet being poorly explored (Salleh & Ahmad, 2017).…”

Section: Introductionmentioning

confidence: 99%

Two new dilactonized glycerol glycosides of the dual anticholinesterase active extract from Ocotea daphnifolia using bioguided fractionation and molecular docking studies

et al. 2022

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The dual inhibition of acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) is considered as an important strategy for the treatment of Alzheimer's disease. In this study, we applied the bioguided fractionations of Ocotea daphinifolia ethyl acetate active extract to furnish a fraction with high inhibitory activity for AChE and BuChE (82% and 92%, respectively). High‐performance liquid chromatography semipreparative purification of this fraction provided two new natural products: 1‐β‐D‐galactopyranosyl‐glycerol‐2,3‐heptanedionate, (1) whose complete chemical structural elucidation was made with spectrometric analysis (MS, 1D, and 2D NMR) and its minor derivative 1‐β‐D‐gulopyranosyl‐glycerol‐2,3‐heptanedionate; (2) which could be characterized by 2D 1H‐13C heteronuclear single‐quantum correlation spectra analysis. Investigation of the intermolecular interactions with cholinesterases was carried out by molecular docking studies, and results suggested that both compounds are capable to interact with the catalytic site of both enzymes. Compounds 1 and 2 interact with residues of catalytic domains and the peripheral anionic binding site of AChE and BuChE. The results are comparable to those achieved with rivastigmine and galantamine. Thus, this study provides evidence for consideration of the glycosylglycerol from O. daphnifolia as new valuable dual cholinesterases inhibitor.

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Section: Introductionmentioning

confidence: 99%