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Title: Synthesis and anti-acetylcholinesterase activity of scopoletin derivatives. Author: Khunnawutmanotham N, Chimnoi N, Saparpakorn P, Techasakul S. Journal: Bioorg Chem; 2016 Apr; 65():137-45. PubMed ID: 26943478. Abstract: A series of scopoletin derivatives incorporated with the pyridinium moiety was synthesized and evaluated for their acetylcholinesterase (AChE) inhibitory activity by the colorimetric Ellman's method. A 2-fluorobenzylpyridinium derivative was the most potent among the tested compounds, with an IC50 value of 0.215±0.015μM, which was greatly improved from that of scopoletin. Docking studies revealed that the scopoletin portion of the mentioned compound was bound to the peripheral anionic site of the AChE, whereas the N-benzylpyridinium residue to the catalytic anionic site.[Abstract] [Full Text] [Related] [New Search]