scholarly journals Synthesis and AChE inhibitory activity of N-glycosyl benzofuran derivatives

2019 ◽  
Vol 25 (1) ◽  
pp. 162-166
Author(s):  
Yu-Ran Wu ◽  
Shu-Ting Ren ◽  
Lei Wang ◽  
Xiu-Jian Liu ◽  
You-Xian Wang ◽  
...  
Keyword(s):  
Carboxylic Acids ◽  
Inhibitory Activity ◽  
Acetylcholinesterase Inhibition ◽  
Inhibition Activity ◽  
Reaction Conditions ◽  
Inhibitory Rate ◽  
Organic Bases ◽  
Ache Inhibitory Activity ◽  
Ellman’S Method

AbstractSix N-glycosyl benzofuran derivatives were synthesized by the catalysis of organic bases and condensation agents. The benzofuran derivatives were obtained by the reaction of various salicylaldehydes in acetone, and then hydrolyzed to the corresponding carboxylic acids. Finally, the target compounds were synthesized by acylation and the reaction conditions were optimized. The acetylcholinesterase (AChE) inhibitory activity of the desired compounds was tested using Ellman’s method. Most of the compounds showed acetylcholinesterase-inhibition activity; N-(2,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)benzofuran-2-carbxamide (5a) showed the best acetylcholinesterase inhibition, with an inhibitory rate of 84%.

Synthesis and bioactivity of novel C2-glycosyl triazole derivatives as acetylcholinesterase inhibitors

2017 ◽  
Vol 23 (3) ◽  
pp. 231-236 ◽  
Author(s):  
Long Yin ◽  
Lei Wang ◽  
Xiu-Jian Liu ◽  
Feng-Chang Cheng ◽  
Da-Hua Shi ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Sodium Hydroxide ◽  
Acetylcholinesterase Inhibitors ◽  
Acetylcholinesterase Inhibition ◽  
Inhibition Activity ◽  
Triazole Derivatives ◽  
Inhibitory Activities ◽  
Ellman’S Method

AbstractNew C2-glycosyl triazole derivatives 6a–l were synthesized by cyclization of glycosyl acylthiosemicarbazides 5 in refluxing 3 N sodium hydroxide aqueous solution. Substrates 5 were obtained by the reaction of glycosyl isothiocyanate 3 with various hydrazides. The acetylcholinesterase (AChE) inhibitory activities of compounds 6 were tested by Ellman’s method. Compounds that exhibited over 85% inhibition were subsequently evaluated for the IC50 values. Compound 6f possesses the best acetylcholinesterase-inhibition activity with IC50 of 1.46±0.25 μg/mL.

scholarly journals Synthesis and anti-acetylcholinesterase activities of novel glycosyl coumarylthiazole derivatives

2020 ◽  
pp. 174751982094835
Author(s):  
You-Xian Wang ◽  
Shu-Hao Liu ◽  
Zhong-Bai Shao ◽  
Lian-Gong Cao ◽  
Kai-Jun Jiang ◽  
...  
Keyword(s):  
Electrospray Ionization ◽  
New Products ◽  
Reaction Conditions ◽  
Inhibitory Rate ◽  
Inhibitory Activities ◽  
Ellman’S Method ◽  
New Compounds ◽  
C Nmr

Eleven glycosyl coumarylthiazole derivatives are synthesized by cyclization and condensation of glycosyl thiourea with 3-bromoacetyl coumarins in ethanol. The reaction conditions are optimized and good yields of products (80%–95%) are obtained. The structures of all new products were confirmed by IR, 1H and 13C NMR, and by HRMS (electrospray ionization). The in vitro acetylcholinesterase (AChE) inhibitory activities of these new compounds are tested by Ellman’s method. Among them, N-(2-acetamido-3,4,6-tri- O-acetyl-2-deoxy-β-D-glucopyranosyl)-4-(6-nitrocoumarinyl)-1,3-thiazole-2-amine showed the best activity with an in vitro AChE inhibitory rate of 58% and an IC50 value of 12 ± 0.38 μg/mL.

Synthesis and bioactivity of novel C2-glycosyl benzofuranylthiazoles derivatives as acetylcholinesterase inhibitors

2019 ◽  
Vol 43 (7-8) ◽  
pp. 257-261
Author(s):  
Lei Wang ◽  
Yu-Ran Wu ◽  
Shu-Ting Ren ◽  
Long Yin ◽  
You-Xian Wang ◽  
...  
Keyword(s):  
Inhibitory Concentration ◽  
Acetylcholinesterase Inhibitors ◽  
Acetylcholinesterase Inhibition ◽  
Inhibition Activity ◽  
Active Compounds ◽  
Inhibitory Activities ◽  
Ellman’S Method

A new series of C2-glycosyl benzofuranylthiazole derivatives was synthesised by the further cyclization of glycosyl thiourea and 2-(bromoacetyl)-benzofuran via Hantzsch’s method. The corresponding 2-(bromoacetyl)-benzofuran derivatives were obtained by the reaction from various salicylaldehydes, and the glycosyl thiourea was prepared through a series of steps from D-Glucosamine. The acetylcholinesterase-inhibitory activities of the products were tested by Ellman’s method. The most active compounds were subsequently evaluated for the 50% inhibitory concentration values. N-(1,3,4,6-tetra-O-benzyl-2-deoxy-β-D-glucopyranosyl)-4-(5-methoxy-benzofuran-2-yl)-1,3-thiazole-2-amine possessed the best acetylcholinesterase-inhibition activity with a 50% inhibitory concentration of 2.03 ± 0.26 μM.

scholarly journals Acetyl-cholinesterase Inhibition by Extracts and Isolated Flavones from Linaria reflexa Desf. (Scrophulariaceae)

2007 ◽  
Vol 2 (7) ◽  
pp. 1934578X0700200 ◽  
Author(s):  
Monica Rosa Loizzo ◽  
Rosa Tundis ◽  
Federica Menichini ◽  
Marco Bonesi ◽  
Giancarlo Antonio Statti ◽  
...  
Keyword(s):  
Dose Response ◽  
Acetylcholinesterase Inhibition ◽  
Activity Relationship ◽  
Cholinesterase Inhibition ◽  
Inhibition Activity ◽  
Response Relationship ◽  
Acetyl Cholinesterase ◽  
Dose Response Relationship ◽  
Structure Activity ◽  
Ellman’S Method

Extracts, linariin, isolinariin A and B obtained from Linaria reflexa Desf. (Scrophulariaceae) were tested for acetylcholinesterase inhibition activity using Ellman's method. A dose-response relationship was observed for all extracts and isolated compounds. Flavones exhibited IC50 values ranging from 0.27 μM to 0.30 μM. The structure-activity relationship was briefly discussed.

scholarly journals Synthesis, characterization, crystal structures, and the biological evaluation of 2-phenylthiazole derivatives as cholinesterase inhibitors

2020 ◽  
pp. 174751982097654
Author(s):  
Da-Hua Shi ◽  
Meng-qiu Song ◽  
Xiao-Dong Ma ◽  
Jia-Bin Su ◽  
Jing Wang ◽  
...  
Keyword(s):  
Cholinesterase Inhibitors ◽  
Docking Study ◽  
Biological Evaluation ◽  
Acetylcholinesterase Inhibition ◽  
Cholinesterase Inhibition ◽  
Resonance Spectroscopy ◽  
Inhibition Activity ◽  
X Ray Diffraction ◽  
Anionic Site ◽  
Ellman’S Method

Four 2-phenylthiazole derivatives are synthesized, characterized, and evaluated as cholinesterase inhibitors. The structures of the 2-phenylthiazole derivatives are confirmed by 1H and 13C nuclear magnetic resonance spectroscopy, single-crystal X-ray diffraction studies, and Hirshfeld surfaces analysis. Hirshfeld surface analysis of the prepared compounds showed C–H···O intermolecular interactions. The cholinesterase inhibition activities of the synthesized compounds are tested by Ellman’s method. [2-(4-Benzyloxyphenyl)-thiazol-4-yl]-(3,5-dimethylpiperidin-1-yl)-methanone showed the best acetylcholinesterase inhibition activity with an IC50 value of 8.86 µM and the best butyrylcholinesterase inhibition activity with an IC50 value of 1.03 µM. A docking study demonstrates that the same compound interacts with the catalytic anionic site and peripheral anionic site of acetylcholinesterase and the catalytic anionic site of butyrylcholinesterase.

scholarly journals An Expedient Synthesis, Acetylcholinesterase Inhibitory Activity, and Molecular Modeling Study of Highly Functionalized Hexahydro-1,6-naphthyridines

2015 ◽  
Vol 2015 ◽  
pp. 1-9 ◽  
Author(s):  
Abdulrahman I. Almansour ◽  
Raju Suresh Kumar ◽  
Natarajan Arumugam ◽  
Alireza Basiri ◽  
Yalda Kia ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Inhibitory Activity ◽  
Sodium Ethoxide ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Binding Interaction ◽  
Phenyl Rings ◽  
Ache Inhibitory Activity ◽  
Methoxy Substituent ◽  
Ellman’S Method

A series of hexahydro-1,6-naphthyridines were synthesized in good yields by the reaction of 3,5-bis[(E)-arylmethylidene]tetrahydro-4(1H)-pyridinones with cyanoacetamide in the presence of sodium ethoxide under simple mixing at ambient temperature for 6–10 minutes and were assayed for their acetylcholinesterase (AChE) inhibitory activity using colorimetric Ellman’s method. Compound4ewith methoxy substituent atortho-position of the phenyl rings displayed the maximum inhibitory activity with IC50value of 2.12 μM. Molecular modeling simulation of4ewas performed using three-dimensional structure ofTorpedo californicaAChE (TcAChE) enzyme to disclose binding interaction and orientation of this molecule into the active site gorge of the receptor.

scholarly journals A Platform for Screening Potential Anticholinesterase Fractions and Components Obtained fromAnemarrhena asphodeloidesBge for Treating Alzheimer’s Disease

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Yu Sun ◽  
Ying Peng ◽  
Lin-Guang Li ◽  
Li-Wei Zheng ◽  
Dong-Ju Lin ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Inhibitory Activity ◽  
Memory Loss ◽  
Symptomatic Treatment ◽  
Ache Inhibitory Activity ◽  
Screening Platform ◽  
Ellman’S Method ◽  
Anemarrhena Asphodeloides ◽  
Ethanol Fraction

Alzheimer’s disease (AD) is a neurodegenerative disease characterized by progressive memory loss and cognitive impairment. Cholinesterase inhibitors are widely used for the symptomatic treatment of Alzheimer’s disease to enhance central cholinergic transmission. In this study, a bioactivity-oriented screening platform based on a modified Ellman’s method and HPLC-QTOF MS technique was developed to rapidly screen active agents ofAnemarrhena asphodeloidesBge. The 60% ethanol fraction from an ethyl acetate extract exhibited the most potential anticholinesterase activity. Fifteen steroid saponins were identified by the mass spectrum, standards and literature reports. Twenty-five compounds were isolated from the active fraction. The results showed that compounds with the C6–C3–C6skeleton probably had both AChE and BuChE inhibitory activities. Xanthone and benzene derivatives exhibited no or little activity. Lignans showed weak BuChE inhibitory activity. The steroidal saponins demonstrated moderate or weak AChE inhibitory activity.

scholarly journals Cholinesterase Inhibition Activity and Molecular Docking Study of Eugenol Derivatives

2021 ◽  
Vol 50 (4) ◽  
pp. 1037-1045
Author(s):  
Khairunisa Mohd Zamli ◽  
Asnuzilawati Asari ◽  
Kooi Yeong Khaw ◽  
Vikneswaran Murugaiyah ◽  
Mariya al-Rashida ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Docking Simulation ◽  
Docking Study ◽  
Protein Docking ◽  
Cholinesterase Inhibition ◽  
Ache Inhibition ◽  
Molecular Docking Study ◽  
Ache Inhibitory Activity ◽  
Inhibition Property ◽  
Ellman’S Method

The study was conducted to explore the anticholinesterase inhibition property of eugenol derived molecules. Ten eugenol derivatives were synthesized and evaluated for the inhibitory activities against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) by Ellman’s method. Most of the tested derivatives showed higher inhibition on BChE than AChE, however, their overall inhibitory activity was weak. In contrast, three derivatives (compounds 3,6,9) showed higher and good AChE inhibitory activity of more than 50% inhibition at 10 μg/mL. Among them, compound 9bearing a ethyl substituent at para position of the benzoyl ring showed the most potent AChE inhibition, with IC50 of 5.64 μg/mL. Ligand-protein docking simulation was also performed for the most active derived molecules (compounds 3,6,9).

scholarly journals Three-Component Access to Functionalized Spiropyrrolidine Heterocyclic Scaffolds and Their Cholinesterase Inhibitory Activity

Molecules ◽  
2020 ◽  
Vol 25 (8) ◽  
pp. 1963 ◽  
Author(s):  
Sarra Boudriga ◽  
Saoussen Haddad ◽  
Vikneswaran Murugaiyah ◽  
Moheddine Askri ◽  
Michael Knorr ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Cycloaddition Reaction ◽  
Docking Study ◽  
X Ray Diffraction ◽  
Molecular Docking Study ◽  
Reaction Conditions ◽  
One Pot ◽  
X Ray ◽  
Cholinesterase Inhibitory Activity ◽  
Ache Inhibitory Activity

A novel one-pot [3+2]-cycloaddition reaction of (E)-3-arylidene-1-phenyl-succinimides, cyclic 1,2-diketones (isatin, 5-chloro-isatin and acenaphtenequinone), and diverse α-aminoacids such as 2-phenylglycine or sarcosine is reported. The reaction provides succinimide-substituted dispiropyrrolidine derivatives with high regio- and diastereoselectivities under mild reaction conditions. The stereochemistry of these N-heterocycles has been confirmed by four X-ray diffraction studies. Several synthetized compounds show higher inhibition on acetylcholinesterase (AChE) than butyrylcholinesterase (BChE). Of the 17 synthesized compounds tested, five exhibit good AChE inhibition with IC50 of 11.42 to 22.21 µM. A molecular docking study has also been undertaken for compound 4n possessing the most potent AChE inhibitory activity, disclosing its binding to the peripheral anionic site of AChE enzymes.

Effect of alkaloid extracted from Huperzia phlegmaria on cognitive deficits scopolamine-induced in mice

2020 ◽  
Vol 16 ◽  
Author(s):  
Dang Kim Thu ◽  
Dao Thi Vui ◽  
Nguyen Thi Ngoc Huyen ◽  
Nguyen Thi Thanh Binh ◽  
Nguyen Thi Huyen ◽  
...  
Keyword(s):  
Cognitive Impairment ◽  
Mouse Brain ◽  
Cognitive Deficits ◽  
Inhibitory Activity ◽  
Water Maze ◽  
Ache Activity ◽  
Y Maze ◽  
Ache Inhibitory Activity ◽  
Kinetic Inhibition ◽  
Brain Tissues

Background: Huperzia phlegmaria has been used for the treatment of neurological disorder. Alkaloids are main bioactive compounds found in Huperzia phlegmaria. We aimed to investigate the acetylcholinesterase (AChE) inhibitory activity in vitro of Huperzia phlegmaria alkaloid extract (HpAE) and protective effects on mice which were induced cognitive deficits by scopolamine. Methods: AChE inhibitory activity and kinetic inhibition mechanism was investigated by Ellman's assay. Mice were administrated orally HpAE (30 mg/kg and 60 mg/kg) for fourteen days, and injected scopolamine at a dose of 1 mg/kg intraperitoneally for four days to induce cognitive impairment. The Y-maze and the Morris water maze were used for evaluating the memory behaviors. Acetylcholine (ACh) levels and AChE activity were measured in brain tissue. Glutathione peroxidase (GPx), superoxide dismutase (SOD) activities, and malondialdehyde (MDA) groups were also evaluated in the mouse brain tissues. Results: Our data showed that HpAE had the strong AChE inhibitory activity with an IC50 value of 5.12 ± 0.48 μg/mL in a concentration-dependent manner. Kinetic inhibition analysis demonstrated that HpPAE inhibited AChE followed the mixed inhibition type with Ki (representing the affinity of the enzyme and inhibitor) was 4.37 ± 0.35 µg/mL. Scopolamine induced the cognitive impairment in Morris Water Maze and Y-maze test along with reduced brain levels of ACh and antioxidant enzyme and increased AChE activity in mouse brain tissues. Treatment with HpAE at both dose (30 mg/kg and 60 mg/kg) decreased the SCP-induced cognitive impairment in both behavioral tests along with decreased acetylcholinesterase activity and MDA level, and increased ACh level and antioxidant enzyme in mouse brain tissues. Conclusion: Our results suggested that the HpAE at both dose (30 mg/kg and 60 mg/kg) may be used for prevent and treatment of Alzheimer’s disease.

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