Monoamine oxidase inhibitory activities of novel 3,4-dihydroquinolin-(1H)-2-one derivatives

Monoamine oxidase inhibitory activities of novel 3,4-dihydroquinolin-(1H)-2-one derivatives

Three 3,4-dihydroquinoline-(1H)-2-one derivatives were synthesized and their monoamine oxidase (MAO) inhibitory activities were evaluated. The calculated IC(50) values revealed that compound Q (N-amino-3,4-dihydroquinoline-(1H)-2-one), which carries a free amine group in the molecule, inhibited rat...

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Bibliographic Details
Published in:Journal of Neural Transmission Vol. 114; no. 6; pp. 717 - 719
Main Authors: Sunal, S G, Yabanoglu, S, Yesilada, A, Ucar, G
Format: Journal Article
Language:English
Published: Austria Springer Nature B.V 01-06-2007
Subjects:
Animals
Binding Sites - drug effects
Binding Sites - physiology
Binding, Competitive - physiology
Enzyme Inhibitors - chemical synthesis
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - pharmacology
Liver - enzymology
Molecular Structure
Monoamine Oxidase - chemistry
Monoamine Oxidase - drug effects
Monoamine Oxidase - metabolism
Quinolones - chemical synthesis
Quinolones - chemistry
Quinolones - pharmacology
Rats
Subcellular Fractions
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Summary:Three 3,4-dihydroquinoline-(1H)-2-one derivatives were synthesized and their monoamine oxidase (MAO) inhibitory activities were evaluated. The calculated IC(50) values revealed that compound Q (N-amino-3,4-dihydroquinoline-(1H)-2-one), which carries a free amine group in the molecule, inhibited rat liver MAO-B competitively and reversibly suggesting that this relatively small compound may interact with the active site channel of the enzyme while the compounds QB (1-(benzlyden-amino)-3,4-dihydroquinoline-(1H)-2-one), PCN (2-(3-cyano-2-oxo-4-phenyl-2H-quinolin-1-yl-N-cyclohexyl-2-(4'-chlorophenyl) acetamide) and MG (tert-butyl-N-[cyclohexylcarbamoyl-(3-hydroxyphenyl)methyl]-N-(2-benzoylphenyl)-carbamate) inhibited rat liver MAO-B non-competitively and irreversibly, suggesting that these compounds may interact with another hydrophobic binding region outside of the active site of the enzyme.
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ISSN:0300-9564
1435-1463
DOI:10.1007/s00702-007-0677-9