ArticleActa pharmacologica Sinica2015
In-silico identification of the binding mode of synthesized adamantyl derivatives inside cholinesterase enzymes.
Article in Acta pharmacologica Sinica, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 16 citations in OpenAlex.
- Chalcone Scaffolds Exhibiting Acetylcholinesterase Enzyme Inhibition: Mechanistic and Computational Investigations.Molecules (Basel, Switzerland) · 2022Article
- Synthesis, Characterization and Biological Evaluation of Metal Adamantyl 2-Pyridylhydrazone Complexes.Molecules (Basel, Switzerland) · 2020Article
- Synthesis, Characterization, Crystal Structure, and DFT Study of a New Square Planar Cu(II) Complex Containing Bulky Adamantane Ligand.Molecules (Basel, Switzerland) · 2018Article
- Novel conjugates of aminoadamantanes with carbazole derivatives as potential multitarget agents for AD treatment.Scientific reports · 2017Article
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
aimTo investigate the binding mode of synthesized adamantly derivatives inside of cholinesterase enzymes using molecular docking simulations.
methodsA series of hybrid compounds containing adamantane and hydrazide moieties was designed and synthesized. Their inhibitory activities against acetylcholinesterase (AChE) and (butyrylcholinesterase) BChE were assessed in vitro. The binding mode of the compounds inside cholinesterase enzymes was investigated using Surflex-Dock package of Sybyl7.3 software.
resultsA total of 26 adamantyl derivatives were synthesized. Among them, adamantane-1-carboxylic acid hydrazide had an almost equal inhibitory activity towards both enzymes, whereas 10 other compounds exhibited moderate inhibitory activity against BChE. The molecular docking studies demonstrated that hydrophobic interactions between the compounds and their surrounding residues in the active site played predominant roles, while hydrophilic interactions were also found. When the compounds were docked inside each enzyme, they exhibited stronger interactions with BChE over AChE, possibly due to the larger active site of BChE. The binding affinities of the compounds for BChE and AChE estimated were in agreement with the experimental data.
conclusionThe new adamantly derivatives selectively inhibit BChE with respect to AChE, thus making them good candidates for testing the hypothesis that BChE inhibitors would be more efficient and better tolerated than AChE inhibitors in the treatment of Alzheimer's disease.
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