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Publication Type : Journal Article
Publisher : ChemMedChem
Source : ChemMedChem, Volume 11, Issue 11, p.1161-71 (2016)
Keywords : Binding Sites, blood-brain barrier, Cell Survival, Chalcones, Halogenation, Hep G2 Cells, Humans, kinetics, Molecular Conformation, Molecular Docking Simulation, Monoamine oxidase, Monoamine Oxidase Inhibitors, Protein Structure, Tertiary, Structure-Activity Relationship
Campus : Kochi
School : School of Pharmacy
Department : Pharmaceutical Chemistry & Analysis
Year : 2016
Abstract : A series of (2E)-1-(5-bromothiophen-2-yl)-3-(para-substituted phenyl)prop-2-en-1-ones (TB1-TB11) was synthesized and tested for inhibitory activity toward human monoamine oxidase (hMAO). All compounds were found to be competitive, selective, and reversible toward hMAO-B except (2E)-1-(5-bromothiophen-2-yl)-3-(4-nitrophenyl)prop-2-en-1-one (TB7) and (2E)-1-(5-bromothiophen-2-yl)-3-(4-chlorophenyl)prop-2-en-1-one (TB8), which were selective inhibitors of hMAO-A. The most potent compound, (2E)-1-(5-bromothiophen-2-yl)-3-[4-(dimethylamino)phenyl]prop-2-en-1-one (TB5), showed the best inhibitory activity and higher selectivity toward hMAO-B, with Ki and SI values of 0.11±0.01 μm and 13.18, respectively. PAMPA assays for all compounds were carried out in order to evaluate the capacity of the compounds to cross the blood-brain barrier. Moreover, the most potent MAO-B inhibitor, TB5, was found to be nontoxic at 5 and 25 μm, with 95.75 and 84.59 % viability among cells, respectively. Molecular docking simulations were carried out to understand the crucial interactions responsible for selectivity and potency.
Cite this Research Publication : Bijo Mathew, Haridas, A., Ucar, G., Baysal, I., Joy, M., Mathew, G. E., Lakshmanan, B., and Jayaprakash, V., “Synthesis, Biochemistry, and Computational Studies of Brominated Thienyl Chalcones: A New Class of Reversible MAO-B Inhibitors.”, ChemMedChem, vol. 11, no. 11, pp. 1161-71, 2016.