Modulation of acetylcholinesterase activity induced by polyoxotungstates

Abstract

The in vitroinfluence of five polyoxotungstates containing various central atoms on acetylcholinesterase (AChE) activity was investigated. K6[PV3W9O40] × 3H2O, K6H2[TiW11CoO40] × 13H2O, (NH4)14[NaP5W30O110] × 31H2O, K7[SiV3W9O40] × 10H2O, and K7[Ti2PW10O40] induced the enzyme inhibition in a concentration-dependent manner. Inhibitory power of the investigated compounds was evaluated using IC50values. K7[SiV3W9O40] × 10H2O affected AChE activity with lowest potency (IC50 = 4.80 × 10-4mol/L). K6H2[TiW11CoO40] × 13H2O and K7[Ti2PW10O40] exhibited high affinity toward the enzyme, inducing half-maximuminhibition at micromolar concentrations (1.14 × 10-6and 1.04 × 10-6mol/L, respectively), while the same effect was achieved in the presence of about fifty times higher concentration of K6[PV3W9O40] × 3H2O. Finally, (NH4)14[NaP5W30O110] × 31H2O was foundas the most potent inhibitor of AChE activity (IC50 = 6.36 × 10-7mol/L), and consequently the most promising candidate for the treatment of neurological diseases associated with acetylcholine leakage.