In this article, a novel amperometric acetylcholine (ACh) biosensor with immobilization of acetylcholinesterase-choline oxidase (AChE-ChO) on electrochemically polymerized polyaniline-polyvinylsulphonate (PANI-PVS) film has been successfully developed for the first time. AChE and ChO enzymes were immobilized on PANI-PVS film by cross-linking with using glutaraldehyde (GA) and bovine serum albumin (BSA). Determination of ACh was carried out by oxidation of enzymatically produced H2O2 at +0.4 V versus Ag/AgCl. Optimum pH and temperature were found to be 8.0 and 60 °C, respectively. The linear part was in the region 1.0 × 10(-7)-6.0 × 10(-7) M (R(2) = 0.990). Storage stability and operation stability of the enzyme electrode were also studied.

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Investigation of acetylcholinesterase (AChE) inhibition potency of some new Schiff base derivatives of tacrine (9-amino-1,2,3,4-tetrahydroacridine) was reported in this paper. Novel Schiff base derivatives of tacrine (3a–g) have been synthesized, and they have been characterized by several methods (FT-IR, 1H-NMR, 13C-NMR, etc.). Then, inhibition effects on AChE by the synthesized compounds have been investigated by the spectrophotometric Ellman method. IC50, Ki, KM and Vmax values and inhibition types have been determined. It was seen that all compounds had the property of a water-soluble reversible AChE inhibitor. Structure 3a was found to be the most potent inhibitor, with the IC50 value of 22.1 ± 1.11  nM (tacrine's IC50 value was calculated as 34.1 nM).