• Archives of Pharmacal Research
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• v.25 no.6
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• pp.817-819
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• 2002

In the course of screening Korean natural products for acetylcholinesterase (AChE) inhibitory activity, it was found that a methanolic extract of the aerial parts of Corydalis incisa (Papaveraceae) showed significant inhibitory effects on AChE. Corynoline isolated from this plant inhibited AChE activity in a dose-dependent manner, and the $IC_{50}$ value of corynoline was $30.6{\;}{\mu}M$. The AChE inhibitory activity of corynoline was reversible and noncompetitive.

• Archives of Pharmacal Research
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• v.26 no.9
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• pp.735-738
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• 2003

The methanolic extract of the twigs of Celtis chinensis was found to show inhibitory activity on acetylcholinesterase (AChE), an enzyme that plays a role in the metabolic hydrolysis of ACh. Bioassay-guided fractionation of the methanolic extract resulted in the isolation of N-p-coumaroyl tyramine. as an inhibitor on AChE. This compound inhibited AChE activity in a dose-dependent manner, and the $IC_50$ value of trans-N-p-coumaroyl tyramine was 34.5 $\mu$g/mL (122 $\mu$M).

• The Journal of Natural Sciences
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• v.19 no.1
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• pp.45-55
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• 2008

Alzheimer's disease is charaterized by the acetylcholine depletion, amyloid b-protein aggregation and neurofibrillary tangles. The prevention of the breakdown of acetylcholine by acetylcholinesterase (AChE) inhibitor has the best clinically therapeutic efficacy for Alzheimer's disease patients. To develop new antidementia alternative drugs or nutraceuticals, methanol extracts of Sorghum bicolor was screened from various extracts of cereals and legumes as a potent AChE inhibitor-containing extract in previous paper. In this paper, physicochemical properties of the methanol extracts was investigated. The methanol extracts was soluble by water, methanol and DMSO and had 215 nm and 282nm of maximum absorption spectra. It was also stable at 20-$100^{\circ}C$ and pH 2.0-10.0 for 1 hr. Test product was prepared by using methanol extracts from Sorghum bicolor and changes of its quality during storge at $20^{\circ}C$ and $40^{\circ}C$ were investigated. It was very stable for 8 weeks at $40^{\circ}C$.

• Journal of Microbiology and Biotechnology
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• v.23 no.2
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• pp.161-166
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• 2013

At present, acetylcholinesterase (AChE) inhibitors are the first group of drugs to treat mild to moderate Alzheimer's disease (AD). Although beneficial in improving cognitive and behavioral symptoms, the effectiveness of AChE inhibitors has been questioned since they do not delay or prevent neurodegeneration in AD patients. Therefore, in the present study, in order to develop new and effective anti-AD agents from lichen products, both the AChE inhibitory and the neuroprotective effects were evaluated. The AChE inhibitory assay was performed based on Ellman's reaction, and the neuroprotective effect was evaluated by using the MTT method on injured PC12 cells. One AChE inhibitor ($IC_{50}$ = 27.1 ${\mu}g/ml$) was isolated by means of bioactivity-guided isolation from the extract of lichen-forming fungus Cladonia macilenta, which showed the most potent AChE inhibitory activity in previous screening experiment. It was then identified as biruloquinone by MS, and $^1H$- and $^{13}C$-NMR analyses. The inhibitory kinetic assay suggested that biruloquinone is a mixed-II inhibitor on AChE. Meanwhile, biruloquinone improved the viability of the $H_2O_2$- and ${\beta}$-amyloid-injured PC12 cells at 1 to 25 ${\mu}g/ml$. The protective effects are proposed to be related to the potent antioxidant activities of biruloquinone. These results imply that biruloquinone has the potential to be developed as a multifunctional anti- AD agent.

• International Journal of Industrial Entomology and Biomaterials
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• v.1 no.1
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• pp.73-78
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• 2000

We investigated some biochemical properties of acetylcholinesterase (AChE) in the Bombyx mori larval head. 1% Triton X-100 (v/v) was suitable for extracting AChE from the silkworm larval head but 1 M NaCl was not suitable. PAGE analysis showed a single band of AChE that was detected by histochemical staining using acetylthiocholine as a substrate. AChE was also partially purified with Sepharose 6B and DEAE-cellulose column. Finally, the specific activity of partially purified enzyme solution was 7.6. The study on inhibitor specificity indicated that the enzyme under study was a true cholinesterase (ChE) or AChE. AChE activity was maximum at the substrate concentration of $5{\times}10^{-4}$ M and the excess substrate inhibited the AChE activity. The optimal pH and temperature were pH 7.0-9.0 and 30-35$^{\circ}C$.

• BMB Reports
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• v.34 no.5
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• pp.440-445
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• 2001

Pesticide waste and chemical stockpiles are posing a potential threat to both Vie environment and human health. There is currently a great effort toward developing effective and economical methods for the detoxification of these toxic organophosphates. In terms of safety and economy, enzymatic biodegradation has been recommended as the most promising tool to detoxify these toxic materials. To develop an enzymatic degradation method to detoxify such toxic organophosphorus compounds, a gene encoding organophosphorus acid anhydrolase (OPAA) from genomic DNA of Alteromonas haloplanktis C was subcloned and expressed. The enzyme consists of a single polypeptide chain with a molecular weight of 48 kDa. It demonstrates strong hydrolyzing activity on sarin, an acetylcholinesterase inhibitor. Moreover, its high activity is sustained for a considerable length of time. It is projected that the recombinant OPAA can be applied as an enzymatic tool that can be used not only for the detoxification of pesticide wastes, but also for the demilitarization of chemical stockpiles.

• Mycobiology
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• v.37 no.3
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• pp.203-206
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• 2009

To develop new antidementia nutraceuticals, a potent acetylcholinesterase (AChE)-inhibiting extract was screened from various extracts of nutritional mushrooms and lichens nutritional and its physicochemical properties were investigated. Among the several extracts tested, methanol extracts of Umbilicaria esculenta fruiting body showed the highest AChE inhibitory activity of 22.4%. U. esculenta AChE inhibitor was maximally extracted when fruiting bodies were treated with 80% methanol at $40^{\circ}C$ for 18 h. The methanol extracts contained 18.9% crude lipid, 18.8% crude protein, and 11.6% total sugar. In addition, they contained 444 mg/g glutamic acid, 44 mg/g histidine, and 41 mg/g aspartic acid. The methanol extracts were soluble in a solution of methanol and 20% dimethylsulfoxide, insoluble in n-hexane, chloroform, and water, and were stable at $20{\sim}60^{\circ}C$ and pH $1.0{\sim}5.0$ for 1 h.

• Bulletin of the Korean Chemical Society
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• v.30 no.4
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• pp.969-971
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• 2009

• YAKHAK HOEJI
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• v.55 no.6
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• pp.473-477
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• 2011

Alzheimer's disease (AD), one of the most common forms of dementia, is a progressive neurodegenerative disorder symptomatically characterized by the decline in memory and cognitive abilities. To date, the successful therapeutic strategy to treat AD is to maintain the levels of acetylcholine (ACh) by inhibiting acetylcholinesterase (AChE) to lead five drugs in clinical use. In this study, several coumarin derivatives were designed based on the lead structure of scopoletin and evaluated for their AChE inhibitory activities.

• Mycobiology
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• v.38 no.1
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• pp.52-57
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• 2010

To develop a potent anti-obesity lipase inhibitor from mushroom, the lipase inhibitory activities of various mushroom extracts were determined. Methanol extracts from Phellinus linteus fruiting body exhibited the highest lipase inhibitory activity (72.8%). The inhibitor was maximally extracted by treatment of a P. linteus fruiting body with 80% methanol at $40^{\circ}C$ for 24 hr. After partial purification by systematic solvent extraction, the inhibitor was stable in the range of $40\sim80^{\circ}C$ and pH 2.0~9.0. In addition to lipase inhibitory activity, the inhibitor showed 59.4% of superoxide dismutase-like activity and 56.3% of acetylcholinesterase inhibitory activity.