In Vitro and In Silico Evaluation of Cholinesterase Inhibition by Alkaloids Obtained from Branches of Abuta panurensis Eichler
Alkaloids are natural products known as ethnobotanicals that have attracted increasing attention due to a wide range of their pharmacological properties. In this study, cholinesterase inhibitors were obtained from branches of Eichler (Menispermaceae), an endemic species from the Amazonian rainforest...
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Published in | Molecules (Basel, Switzerland) Vol. 27; no. 10; p. 3138 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Switzerland
MDPI AG
13.05.2022
MDPI |
Subjects | |
Online Access | Get full text |
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Summary: | Alkaloids are natural products known as ethnobotanicals that have attracted increasing attention due to a wide range of their pharmacological properties. In this study, cholinesterase inhibitors were obtained from branches of
Eichler (Menispermaceae), an endemic species from the Amazonian rainforest. Five alkaloids were isolated, and their structure was elucidated by a combination of 1D and 2D
H and
C NMR spectroscopy, HPLC-MS, and high-resolution MS: Lindoldhamine isomer
/
569.2674 (
), stepharine
/
298.1461 (
), palmatine
/
352.1616 (
), 5-
-methylmaytenine
/
420.2669 (
) and the
-
-feruloyltyramine
/
314.1404 (
). The compounds
,
, and
were isolated from
for the first time. Interaction of the above-mentioned alkaloids with acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes was investigated in silico by molecular docking and molecular dynamics. The molecules under investigation were able to bind effectively with the active sites of the AChE and BChE enzymes. The compounds
-
demonstrated in vitro an inhibitory effect on acetylcholinesterase with IC
values in the range of 19.55 µM to 61.24 µM. The data obtained in silico corroborate the results of AChE enzyme inhibition. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1420-3049 1420-3049 |
DOI: | 10.3390/molecules27103138 |