TMTFA has a reactive
ketone group that can covalently bind to the
serine residue in the active site of acetylcholinesterase. This is due to the electron-withdrawing
trifluoromethyl group on the
carbonyl group.[5]
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^Butini S, Campiani G, Borriello M, Gemma S, Panico A, Persico M, Catalanotti B, Ros S, Brindisi M, Agnusdei M, Fiorini I, Nacci V, Novellino E, Belinskaya T, Saxena A, Fattorusso C. Exploiting protein fluctuations at the active-site gorge of human cholinesterases: further optimization of the design strategy to develop extremely potent inhibitors. J Med Chem. 2008 Jun 12;51(11):3154-70.
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^Harel, Michal; Quinn, Daniel M.; Nair, Haridasan K.; Silman, Israel; Sussman, Joel L. (January 1996). "The X-ray Structure of a Transition State Analog Complex Reveals the Molecular Origins of the Catalytic Power and Substrate Specificity of Acetylcholinesterase". Journal of the American Chemical Society. 118 (10): 2340–2346.
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