Abstract
Testosterone and ten of its metabolites were examined as inhibitors of butyrylcholinesterase. A significant enzyme inhibition activity (IC50 = 1.55 μM) 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.
Acknowledgements
We are grateful to the Deanship of Scientific Research at the University of Jordan (Jordan) for financial support. We also acknowledge the Higher Education Commission (Pakistan) for financial support to A. Al-Aboudi under the short-term Foreign Faculty program.
Declaration of interest: The authors report no conflicts of interest. The authors alone are responsible for the content and writing of the paper.