Yang_2018_Mikrochim.Acta_185_132

A new water soluble fluorescent coronene probe (CTCA) was synthesized and is shown to display strong fluorescence (with excitation/emission maxima at 313/450 nm) in aqueous solution. Dopamine was oxidized under air to form polydopamine (PDA) which quenches the fluorescence of CTCA. The enzyme acetylcholinesterase (AChE) is known catalyze the hydrolysis of acetylthiocholine to produce thiocholine. Thiocholine inhibits the polymerization of DA, and this leads to recovery in CTCA fluorescence. These findings form the basis for a new method for detection of AChE activity. The assay has a detection limit as low as 0.05 mU.mL(-1) of AChE. It is highly selective, and other enzymes do no noticeably interfere. It was applied to the determination of AChE activity in (spiked) human serum, and of AChE inhibitors in (spiked) lake water samples. Graphical abstract Controlled synthesis of polydopamine for the highly sensitive and selective sensing of AChE activity is reported for the first time.