Computational studies of acetylcholinesterase complexed with fullerene derivatives: a new insight for Alzheimer disease treatment
Language English Country England, Great Britain Media print-electronic
Document type Journal Article
- Keywords
- AChE inhibition, Alzheimer’s disease, docking, fullerene derivatives, molecular modeling, theoretical methodologies,
- MeSH
- Acetylcholinesterase chemistry metabolism MeSH
- Cholinesterase Inhibitors chemistry metabolism pharmacology MeSH
- Fullerenes chemistry metabolism pharmacology MeSH
- Molecular Conformation * MeSH
- Models, Molecular * MeSH
- Drug Design MeSH
- Molecular Dynamics Simulation MeSH
- Molecular Docking Simulation MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Acetylcholinesterase MeSH
- Cholinesterase Inhibitors MeSH
- fullerene C60 MeSH Browser
- Fullerenes MeSH
Here, we propose five fullerene (C60) derivatives as new drugs against Alzheimer's disease (AD). These compounds were designed to act as new human acetylcholinesterase (HssAChE) inhibitors by blocking its fasciculin II (FASII) binding site. Docking and molecular dynamic results show that our proposals bind to the HssAChE tunnel entrance, forming stable complex, and further binding free energy calculations suggest that three of the derivatives proposed here could be potent HssAChE inhibitors. We found a region formed by a set of residues (Tyr72, Asp74, Trp286, Gln291, Tyr341, and Pro344) which can be further exploited in the drug design of new inhibitors of HssAChE based on C60 derivatives. Results presented here report for the first time by a new class of molecules that can become effective drugs against AD.
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