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Synthesis, in vitro enzyme activity and molecular docking studies of new benzylamine-sulfonamide derivatives as selective MAO-B inhibitors
- Source :
- Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 35, Iss 1, Pp 1422-1432 (2020)
- Publication Year :
- 2020
- Publisher :
- Taylor & Francis Group, 2020.
-
Abstract
- Many studies have been conducted on the selective inhibition of human monoamine oxidase B (hMAO-B) enzyme using benzylamine-sulphonamide derivatives. Using various chemical modifications on BB-4h, which was reported previously by our team and showed a significant level of MAO-B inhibition, novel benzylamine-sulphonamide derivatives were designed, synthesised, and their MAO inhibition potentials were evaluated. Among the tested derivatives, compounds 4i and 4t achieved IC50 values of 0.041 ± 0.001 µM and 0.065 ± 0.002 µM, respectively. The mechanism of hMAO-B inhibition by compounds 4i and 4t was studied using Lineweaver–Burk plot. The nature of inhibition was also determined to be non-competitive. Cytotoxicity tests were conducted and compounds 4i and 4t were found to be non-toxic. Molecular docking studies were also carried out for compound 4i, which was found as the most potent agent, within hMAO-B catalytic site.
Details
- Language :
- English
- ISSN :
- 14756366 and 14756374
- Volume :
- 35
- Issue :
- 1
- Database :
- Directory of Open Access Journals
- Journal :
- Journal of Enzyme Inhibition and Medicinal Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.5c8f89ef95f14cababecb6d378950914
- Document Type :
- article
- Full Text :
- https://doi.org/10.1080/14756366.2020.1784892