Potent inhibition of acetylcholinesterase by sargachromanol I from Sargassum siliquastrum and by selected natural compounds

Lee, Jae Pil; Kang, Myung-Gyun; Lee, Joon Yeop; Oh, Jong Min; Baek, Seung Cheol; Leem, Hyun Hee; Park, Daeui; Cho, MyoungLae; Kim, Hoon

doi:10.1016/j.bioorg.2019.103043

Cited by 55 publications

(50 citation statements)

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“…As regards other natural compounds, inhibition of BChE by GC was greater than that by boldine (IC 50 = 321 µM) [ 45 ], hyperforin and hyuganin C (IC 50 = 141.60 and 38.86 μM, respectively) [ 46 ], cremaphenanthrene F (14.62) [ 47 ], scopoletin (IC 50 = 9.11 µM) [ 48 ], and broussonin A and sagachromanol I (IC 50 = 7. 50 and 10.79 µM, respectively) [ 49 ], but less than those of norditerpenoids isograndifoliol and (1 R ,15 R )-1-acetoxycryptotanshinone (IC 50 = 0.9 and 2.4 µM, respectively) [ 50 ]. Notably, these IC 50 values were much greater than those for AChE inhibition by tannic acid (IC 50 = 0.087 µM) [ 51 ], or hesperidin (IC 50 = 0.00345 µM) [ 52 ].…”

Section: Discussionmentioning

confidence: 99%

“…Enzymes (recombinant human MAO-A and MAO-B, AChE from Electrophorus electricus , and BChE from equine serum), substrates (kynuramine and benzylamine, acetylthiocholine iodide (ATCI), S -butyrylthiocholine iodide (BTCI)), inhibitors (toloxatone, lazabemide, and tacrine), and other chemicals including 5,5′-dithiobis(2-nitrobenzoic acid) (DTNB) were purchased from Sigma-Aldrich (St. Louis, MO, USA) [ 49 , 58 ]. The irreversible inhibitors (clorgyline and pargyline) were obtained from BioAssay Systems (Hayward, CA, USA) [ 59 ].…”

Section: Methodsmentioning

confidence: 99%

“…AChE activity was assayed continuously for 10 min at 412 nm using 0.2 U/mL of enzyme in the presence of 0.5 mM DTNB and 0.5 mM ATCI in 0.5 mL of reaction mixture, as previously described [ 49 , 58 ], based on the method developed by Ellman et al [ 62 ]. BChE activity was assayed using the same method as AChE, except using BTCI [ 49 ]. Substrate concentrations of BTCI for BChE and benzylamine for MAO-B were 2.3- and 2.1-fold of the respective K m values (0.22 and 0.14 mM).…”

Section: Methodsmentioning

confidence: 99%

“…IC 50 values of compounds exhibiting >50% inhibition were determined. Kinetic parameters, inhibition types, and K i values were determined for the most potent inhibitors, i.e., GC for BChE and LG for MAO-B, as previously described [ 49 , 58 ]. The kinetics of BChE and MAO-B inhibitions were investigated at five different substrate concentrations; 0.05, 0.1, 0.25, 0.5 or 1.0 mM for BChE, and 0.03, 0.06, 0.15, 0.3, or 0.6 mM for MAO-B.…”

Section: Methodsmentioning

confidence: 99%

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

et al. 2020

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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 Ki value of 4.47 µM, and LG was a reversible competitive inhibitor of MAO-B with a Ki value of 0.024 µM. Docking simulations showed that the binding affinity of GC for BChE (−7.8 kcal/mol) was greater than its affinity for AChE (−7.1 kcal/mol), and suggested that GC interacted with BChE at Thr284 and Val288 by hydrogen bonds (distances: 2.42 and 1.92 Å, respectively) beyond the ligand binding site of BChE, but that GC did not form hydrogen bond with AChE. The binding affinity of LG for MAO-B (−8.8 kcal/mol) was greater than its affinity for MAO-A (−7.9 kcal/mol). These findings suggest GC and LG should be considered promising compounds for the treatment of Alzheimer’s disease with multi-targeting activities.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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

et al. 2020

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“…AChE activity was assayed continuously for 10 min at 412 nm using ~ 0.2 U/mL of enzyme in the presence of 0.5 mM DTNB and 0.5 mM ATCI in 0.5 ml of reaction mixture, as previously described [49,58], based on the method developed by Ellman et al [62]. BChE activity was assayed using the same method as AChE, except using BTCI [49]. Substrate concentrations of BTCI for BChE and benzylamine for MAO-B were 2.3and 2.1-fold of the respective Km values (0.22 and 0.14 mM).…”

Section: Chemicals and Enzyme Assaysmentioning

confidence: 99%

Inhibition of Butyrylcholinesterase by Glycyrol, a Coumarin, Isolated from Glycyrrhiza Uralensis

Jeong¹,

Kang²,

Lee³

et al. 2020

Preprint

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Eight compounds were isolated from the roots of Glycyrrhiza uralensis and tested for cholinesterase (ChE) and monoamine oxidase (MAO) inhibitory activities. 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 (&gt; 40 µM). GC was a reversible, noncompetitive inhibitor of BChE with a Ki value of 4.47 µM, and LG was a reversible competitive inhibitor of MAO-B with a Ki value of 0.024 µM. Docking simulations showed that the binding affinity of GC for BChE (-7.8 kcal/mol) was greater than its affinity for AChE (-7.1 kcal/mol), and suggested that GC interacted with BChE at Thr284 and Val288 by hydrogen bonds (distances: 2.42 and 1.92 Å, respectively) beyond the ligand binding site of BChE, but that GC did not form hydrogen bond with AChE. The binding affinity of LG for MAO-B (-8.8 kcal/mol) was greater than its affinity for MAO-A (-7.9 kcal/mol). These findings suggest GC and LG should be considered promising compounds for the treatment of Alzheimer’s disease with multi-targeting activities.

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Maternal exposure to glyphosate‐based herbicide promotes changes in the muscle structure of C57BL/6 mice offspring

Barbosa

Zazula

Oliveira

et al. 2022

The Anatomical Record

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Glyphosate (GBH) is a worldwide consumption pesticide and is used in the formulation of Roundup®, one of the most commercialized herbicides in the world. Maternal exposure to this herbicide can promote changes and adaptations in the offspring; however, the effects on skeletal muscle are poorly understood. In this sense, the present study sought to evaluate the effect of exposure to GBH on the characteristics of the soleus (SOL) and extensor digitorum longus (EDL) muscles. C57BL/6 pregnant female mice were divided into two groups: control (CTL) receiving water and glyphosate (GBH; n = 6) receiving 0.5% glyphosate. Male puppies were designated according to the group to which the mothers belonged, such as CTL‐F1 and GBH‐F1 and then euthanized at 150 days of age. There was a reduction in body weight and nasoanal length of animals exposed to GBH, while there was an increase in EDL weight, reduction in the proportion of fibers and number of nuclei, and an increase in the connective tissue of the SOL. The animals exposed to GBH presented higher values of body characteristics, mainly adiposity gain, while they presented a reduction in neuromuscular junctions (NMJ), and an increase in fibrosis in the SOL muscle, while there was a reduction in the number of nuclei, and an increase in the weight of the EDL muscle. These findings indicate that glyphosate can promote changes in the offspring's body growth, the deposition of adipose panicles and its effects on muscle can lead to changes in the structure and functioning of this tissue.

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Potent inhibition of acetylcholinesterase by sargachromanol I from Sargassum siliquastrum and by selected natural compounds

Cited by 55 publications

References 63 publications

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

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

Inhibition of Butyrylcholinesterase by Glycyrol, a Coumarin, Isolated from Glycyrrhiza Uralensis

Maternal exposure to glyphosate‐based herbicide promotes changes in the muscle structure of C57BL/6 mice offspring

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