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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 [J Enzyme Inhib Med Chem] 2020 Dec; Vol. 35 (1), pp. 1422-1432. - Publication Year :
- 2020
-
Abstract
- Many studies have been conducted on the selective inhibition of human monoamine oxidase B ( h MAO-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 IC <subscript>50</subscript> values of 0.041 ± 0.001 µM and 0.065 ± 0.002 µM, respectively. The mechanism of h MAO-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 h MAO-B catalytic site.
- Subjects :
- Animals
Benzylamines chemistry
Dose-Response Relationship, Drug
Humans
Mice
Molecular Structure
Monoamine Oxidase Inhibitors chemical synthesis
Monoamine Oxidase Inhibitors chemistry
NIH 3T3 Cells
Structure-Activity Relationship
Sulfanilamide chemistry
Benzylamines pharmacology
Molecular Docking Simulation
Monoamine Oxidase metabolism
Monoamine Oxidase Inhibitors pharmacology
Sulfanilamide pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 1475-6374
- Volume :
- 35
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of enzyme inhibition and medicinal chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 32602377
- Full Text :
- https://doi.org/10.1080/14756366.2020.1784892