Synthesis of 3-aminocoumarin-N-benzylpyridinium conjugates with nanomolar inhibitory activity against acetylcholinesterase

• Nisachon Khunnawutmanotham,
• Cherdchai Laongthipparos,
• Patchreenart Saparpakorn,
• Nitirat Chimnoi and
• Supanna Techasakul

Beilstein J. Org. Chem. 2018, 14, 2545–2552, doi:10.3762/bjoc.14.231

• target enzyme by a dual binding site mechanism whereby the coumarin portion binds with the peripheral anionic site while the N-benzylpyridinium residue binds with the catalytic anionic site of the enzyme. Keywords: acetylcholinesterase inhibitor; 3-aminocoumarin; N-benzylpyridinium; dual binding site

• that may be useful for binding with this enzyme. Herein, we report our progress on the synthesis, biological evaluation, and molecular docking of 3-aminocoumarin linked with the benzylpyridinium moiety through an amide bond. Results and Discussion Chemistry The target 3-aminocoumarin-N-benzylpyridinium

• and of the amide group to Phe338 in the CAS and between the nitrogen atom of the amide group to Tyr124 in the PAS were the key interactions of the synthesized 3-aminocoumarin-N-benzylpyridinium conjugates in the binding pocket of AChE. Conclusion A series of 3-amino-6,7-dimethoxycoumarins conjugated

Multicomponent reaction access to complex quinolines via oxidation of the Povarov adducts

• Esther Vicente-García,
• Rosario Ramón,
• Sara Preciado and
• Rodolfo Lavilla

Beilstein J. Org. Chem. 2011, 7, 980–987, doi:10.3762/bjoc.7.110

• resulting from the reaction between 3-aminocoumarin, aldehydes and cyclic enol ethers have been oxidized with different types of reagents, such as bromide, palladium, DDQ, sodium periodate, manganese dioxide or CAN, but in all cases the main product was the elimination–oxidation compound [29]. Finally