Publication Type : Journal Article
Publisher : Biomed Pharmacothe
Source : Biomed Pharmacother, Volume 106, p.8-13 (2018)
Url : https://pubmed.ncbi.nlm.nih.gov/29940538/
Keywords : Binding Sites, Chalcones, Humans, Imidazoles, kinetics, Molecular Docking Simulation, Molecular Structure, Monoamine oxidase, Monoamine Oxidase Inhibitors, Protein Binding, Structure-Activity Relationship
Campus : Kochi
School : School of Pharmacy
Department : Pharmaceutical Chemistry & Analysis
Year : 2018
Abstract : In the present study, series of eleven (2E)-1-[4-(1H-imidazol-1-yl)substituted phenyl]-3-phenylprop-2-en-1-one (IM1-IM11) derivatives were synthesized and evaluated as inhibitors of recombinant human monoamine oxidase (MAO) A and B. The results indicate that (2E)-3-[4-(dimethylamino) phenyl]-1-[4-(1H-imidazol-1-yl) phenyl] prop-2-en-1-one (IM5) is a nonselective and reversible competitive inhibitor of MAO-A and MAO-B with IC values of 0.30 ± 0.010 and 0.40 ± 0.017 μM, respectively ; those of (2E)-1-[4-(1H-imidazol-1-yl) phenyl]-3-(4-methylphenyl) prop-2-en-1-one (IM4) were 1.06 ± 0.090 and 0.32 ± 0.021 μM, respectively. Kinetic studies document that both IM5 and IM4 are competitive inhibitors of MAO-A and MAO-B with Ki value of 0.11 ± 0.0085 and 0.085 ± 0.0064 μM, respectively. Molecular docking studies of lead compounds further explained the binding modes in the inhibitor binding cavity of both MAO-A and MAO-B.
Cite this Research Publication : R. Sasidharan, Baek, S. Cheol, Leelabaiamma, M. Sreedharan, Kim, H., and Bijo Mathew, “Imidazole bearing chalcones as a new class of monoamine oxidase inhibitors.”, Biomed Pharmacother, vol. 106, pp. 8-13, 2018.