Alkaloids from Peumus boldus and their Acetylcholinesterase, Butyrylcholinesterase and Prolyl Oligopeptidase Inhibition Activity

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11160%2F15%3A10312241" target="_blank" >RIV/00216208:11160/15:10312241 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60162694:G44__/15:43875372

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Alkaloids from Peumus boldus and their Acetylcholinesterase, Butyrylcholinesterase and Prolyl Oligopeptidase Inhibition Activity

Popis výsledku v původním jazyce

Eleven isoquinoline alkaloids (1-11) were isolated from dried leaves of Peumus boldus Mol. by standard chromatographic methods. The chemical structures were elucidated by MS, and 1D and 2D NMR spectroscopic analysis, and by comparison with literature data. Compounds isolated in sufficient amount were evaluated for their acetylcholinesterase, and butyrylcholinesterase inhibition activity using Ellman's method. In the prolyl oligopeptidase assay, Z-Gly-Pro-p-nitroanilide was used as substrate. Promising butyrylcholinesterase inhibition activities were demonstrated by two bthizylisoquinoline alkaloids, reticuline (8) and N-methylcoclaurine (9), with IC50 values of 33.6 +/- 3.0 mu M and 15.0 +/- 1.4 mu M, respectively. Important prolyl oligopeptidase inhibition activities were shown by N-methyllaurotetanine (6) and sinoacutine (4) with IC50 values of 135.4 +/- 23.2 mu M and 143.1 +/- 25.4 mu M, respectively. Other tested compounds were considered inactive.

Název v anglickém jazyce

Alkaloids from Peumus boldus and their Acetylcholinesterase, Butyrylcholinesterase and Prolyl Oligopeptidase Inhibition Activity

Popis výsledku anglicky

Eleven isoquinoline alkaloids (1-11) were isolated from dried leaves of Peumus boldus Mol. by standard chromatographic methods. The chemical structures were elucidated by MS, and 1D and 2D NMR spectroscopic analysis, and by comparison with literature data. Compounds isolated in sufficient amount were evaluated for their acetylcholinesterase, and butyrylcholinesterase inhibition activity using Ellman's method. In the prolyl oligopeptidase assay, Z-Gly-Pro-p-nitroanilide was used as substrate. Promising butyrylcholinesterase inhibition activities were demonstrated by two bthizylisoquinoline alkaloids, reticuline (8) and N-methylcoclaurine (9), with IC50 values of 33.6 +/- 3.0 mu M and 15.0 +/- 1.4 mu M, respectively. Important prolyl oligopeptidase inhibition activities were shown by N-methyllaurotetanine (6) and sinoacutine (4) with IC50 values of 135.4 +/- 23.2 mu M and 143.1 +/- 25.4 mu M, respectively. Other tested compounds were considered inactive.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

FR - Farmakologie a lékárnická chemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Natural Product Communications

ISSN

1934-578X

e-ISSN

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Svazek periodika

10

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

4

Strana od-do

577-580

Kód UT WoS článku

000353424800010

EID výsledku v databázi Scopus

2-s2.0-84933513166