Abstract
Testosterone and ten of its metabolites were examined as inhibitors of butyrylcholinesterase. A significant enzyme inhibition activity (IC(50) = 1.55 microM) was observed for androst-4-en-3,7-dione. The kinetic parameters of butyrylcholinesterase inhibition were determined and molecular docking was carried out in order to develop a better understanding of the inhibitor-enzyme interactions. The results showed that the inhibition was non-competitive, stabilized mainly by hydrogen bonds and hydrophobic interactions between the inhibitor and butyrylcholinesterase.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Androstenedione / chemistry
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Androstenedione / pharmacology*
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Binding Sites
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Butyrylcholinesterase / metabolism*
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Cholinesterase Inhibitors / chemistry
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Cholinesterase Inhibitors / pharmacology*
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Hydrogen Bonding
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Hydrophobic and Hydrophilic Interactions
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Inhibitory Concentration 50
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Kinetics
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Models, Molecular
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Protein Conformation
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Structure-Activity Relationship
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Testosterone / chemistry
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Testosterone / pharmacology*
Substances
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Cholinesterase Inhibitors
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Enzyme Inhibitors
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Testosterone
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Androstenedione
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Butyrylcholinesterase