Inhibition of Butyrylcholinesterase and Human Monoamine Oxidase-B by the Coumarin Glycyrol and Liquiritigenin Isolated from Glycyrrhiza uralensis.

ABSTRACT: Eight compounds were isolated from the roots of Glycyrrhiza uralensis and tested for cholinesterase (ChE) and monoamine oxidase (MAO) inhibitory activities. The coumarin glycyrol (GC) effectively inhibited butyrylcholinesterase (BChE) and acetylcholinesterase (AChE) with IC₅₀ values of 7.22 and 14.77 µM, respectively, and also moderately inhibited MAO-B (29.48 µM). Six of the other seven compounds only weakly inhibited AChE and BChE, whereas liquiritin apioside moderately inhibited AChE (IC₅₀ = 36.68 µM). Liquiritigenin (LG) potently inhibited MAO-B (IC₅₀ = 0.098 µM) and MAO-A (IC₅₀ = 0.27 µM), and liquiritin, a glycoside of LG, weakly inhibited MAO-B (>40 µM). GC was a reversible, noncompetitive inhibitor of BChE with a K_i valu

SUBMITTER: Jeong GS 

PROVIDER: S-EPMC7504216 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature