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.

scholarly journals DNA Topoisomerase I Inhibitory Activity of Quinochalcone C-glycosides from the Florets of Carthamus tinctorius

2017 ◽  
Vol 12 (11) ◽  
pp. 1934578X1701201
Author(s):  
Shi-Jun Yue ◽  
Wen-Xiao Wang ◽  
Cheng Qu ◽  
Lan-Ting Xin ◽  
Yu-Ping Tang ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Dna Cleavage ◽  
Topoisomerase I ◽  
Docking Study ◽  
Carthamus Tinctorius ◽  
In Vitro Cytotoxicity ◽  
Molecular Docking Study ◽  
Dna Topoisomerase ◽  
Cleavage Complex

The DNA topoisomerase (Topo) I inhibitory activity of six quinochalcone C-glycosides (QCGs) isolated from the florets of Carthamus tinctorius were evaluated in vitro. Among them, anhydrosafflor yellow B (AHSYB, 4) and carthorquinoside B (6) could inhibit DNA Topo I at concentrations as low as 100 μM. Molecular docking study revealed that both of them have the capacity to stabilize Topo I-DNA cleavage complex in silico interacting with the essential binding sites, such as Arg364, Thr718 and TGP11. Besides, both compounds 4 and 6 exhibited no antitumor activity by in vitro cytotoxicity assays.

scholarly journals A New Tyrosinase Inhibitor from the Red Alga Symphyocladia latiuscula (Harvey) Yamada (Rhodomelaceae)

Marine Drugs ◽  
2019 ◽  
Vol 17 (5) ◽  
pp. 295 ◽  
Author(s):  
Pradeep Paudel ◽  
Aditi Wagle ◽  
Su Hui Seong ◽  
Hye Jin Park ◽  
Hyun Ah Jung ◽  
...  
Keyword(s):  
Methyl Ether ◽  
Inhibitory Activity ◽  
Biological Activities ◽  
Docking Study ◽  
Red Alga ◽  
Moderate Activity ◽  
Molecular Docking Study ◽  
Tyrosinase Inhibitory Activity ◽  
Ic50 Values ◽  
Catalytic Hydrogen

A marine red alga, Symphyocladia latiuscula (Harvey) Yamada (Rhodomelaceae), is a rich source of bromophenols with a wide array of biological activities. This study investigates the anti-tyrosinase activity of the alga. Moderate activity was demonstrated by the methanol extract of S. latiuscula, and subsequent column chromatography identified three bromophenols: 2,3,6-tribromo-4,5-dihydroxybenzyl methyl alcohol (1), 2,3,6-tribromo-4,5-dihydroxybenzyl methyl ether (2), and bis-(2,3,6-tribromo-4,5-dihydroxybenzyl methyl ether) (3). Bromophenols 1 and 3 exhibited potent competitive tyrosinase inhibitory activity against l-tyrosine substrates, with IC50 values of 10.78 ± 0.19 and 2.92 ± 0.04 μM, respectively. Against substrate l-3,4-dihydroxyphenylalanine (l-DOPA), compounds 1 and 3 demonstrated moderate activity, while 2 showed no observable effect. The experimental data were verified by a molecular docking study that found catalytic hydrogen and halogen interactions were responsible for the activity. In addition, compounds 1 and 3 exhibited dose-dependent inhibitory effects in melanin and intracellular tyrosinase levels in α-melanocyte-stimulating hormone (α-MSH)-induced B16F10 melanoma cells. Compounds 3 and 1 were the most effective tyrosinase inhibitors. In addition, increasing the bromine group number increased the mushroom tyrosinase inhibitory activity.

Synthesis of Novel Benzimidazole and Benzothiazole Derivatives Bearing a 1,2,3-triazole Ring System and their Acetylcholinesterase Inhibitory Activity

2017 ◽  
Vol 41 (1) ◽  
pp. 30-35 ◽  
Author(s):  
Laleh Faraji ◽  
Shiva Shahkarami ◽  
Hamid Nadri ◽  
Alireza Moradi ◽  
Mina Saeedi ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Docking Simulation ◽  
Triazole Ring ◽  
Copper Catalysts ◽  
Inhibitory Effect ◽  
Ring System ◽  
Benzothiazole Derivatives ◽  
Ache Inhibitory Activity ◽  
Group A

A series of 20 novel benzimidazole and benzothiazole derivatives linked to a 1,2,3-triazole ring system was synthesised, characterised and evaluated for in vitro acetylcholinesterase (AChE) inhibitory activity. Several copper catalysts and solvents were screened to establish the optimal conditions for the preparation of the target compounds. Three different linkers were used to optimise the enzyme inhibitory effect. Out of the 20 compounds, 13 showed some AChE inhibition. The most potent compound, which showed 84% inhibition at 100 μM, contained a 1-(2-fluorobenzyl)-1,2,3-triazole linked to a benzimidazole group. A docking simulation study showed that the most active compound bound preferentially to the catalytic anionic subsite of the AChE enzyme.

Synthesis, molecular docking study and thymidine phosphorylase inhibitory activity of 3-formylcoumarin derivatives

2018 ◽  
Vol 78 ◽  
pp. 17-23 ◽  
Author(s):  
Muhammad Taha ◽  
Syed Adnan Ali Shah ◽  
Muhammad Afifi ◽  
Syahrul Imran ◽  
Sadia Sultan ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Inhibitory Activity ◽  
Thymidine Phosphorylase ◽  
Docking Study ◽  
Molecular Docking Study

scholarly journals Virtual molecular docking study of some novel carboxamide series as new anti-tubercular agents

2020 ◽  
Vol 11 (1) ◽  
pp. 30-36 ◽  
Author(s):  
Mustapha Abdullahi ◽  
Adamu Uzairu ◽  
Gideon Adamu Shallangwa ◽  
David Ebuka Arthur ◽  
Bello Abdullahi Umar ◽  
...  
Keyword(s):  
Binding Energy ◽  
Active Sites ◽  
Docking Simulation ◽  
Docking Study ◽  
Amino Acid Residues ◽  
Ant System ◽  
Molecular Docking Study ◽  
Molegro Virtual Docker ◽  
Chemical Structures ◽  
Hydrogen Bond Interactions

A virtual docking simulation study was performed on thirty-five newly discovered compounds of N-(2-phenoxy) ethyl imidazo[1,2-a] pyridine-3-carboxamide (IPA), to explore their theoretical binding energy and pose with the active sites of the Mycobacterium tuberculosis target (DNA gyrase). The chemical structures of the compounds were drawn correctly with ChemDraw Ultra software, and then geometrically optimized at DFT level of theory with Spartan 14 software package. Consequently, the docking analysis was carried out using Molegro Virtual Docker (MVD). Five complexes (Complex 5, 24, 25, 33 and 35) with high binding energy were selected to examine their binding pose with the active sites of the protein. The docking results suggested a good MolDock score (≥ -90 kcal/mol) and Protein-Ligand ANT System (PLANTS) score (≥ -60 kcal/mol) which depicted that the compounds can efficiently bind with the active sites of the target. However, compound 5 has the best binding pose with the MolDock score of -140.476 kcal/mol which formed three hydrogen bond interactions with the Gln 538, Ala 531, and Ala 533 amino acid residues. This research gives a firsthand theoretical knowledge to improve the binding efficiency of these compounds with the target.

Sign in / Sign up

Export Citation Format

Share Document