Butyrylcholinesterase inhibitory activity of testosterone and some of its metabolites.
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.
Al-Aboudi
Amal
A
Department of Chemistry, University of Jordan, Amman, Jordan. alaboudi@ju.edu.jo
Odeh
Hana
H
Khalid
Asaad
A
Naz
Qamar
Q
Choudhary
M Iqbal
MI
D000735:Androstenedione / Q000737:chemistry / Q000494:pharmacology*; D001665:Binding Sites; D002091:Butyrylcholinesterase / Q000378:metabolism*; D002800:Cholinesterase Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D020128:Inhibitory Concentration 50; D007700:Kinetics; D008958:Models, Molecular; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013739:Testosterone / Q000737:chemistry / Q000494:pharmacology*
D002800:Cholinesterase Inhibitors; D004791:Enzyme Inhibitors; D013739:Testosterone; D000735:Androstenedione; D002091:Butyrylcholinesterase