State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, 130022, People's Republic of China.
University of Chinese Academy of Sciences, Beijing, 100049, People's Republic of China.
Mikrochim Acta. 2018 Jan 25;185(2):132. doi: 10.1007/s00604-018-2678-9.
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 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.
一种新的水溶性荧光蒄（CTCA）被合成，并被证明在水溶液中显示出强荧光（激发/发射最大值为 313/450nm）。多巴胺在空气中氧化形成聚多巴胺（PDA），猝灭 CTCA 的荧光。已知酶乙酰胆碱酯酶（AChE）催化乙酰硫代胆碱水解生成硫代胆碱。硫代胆碱抑制 DA 的聚合，这导致 CTCA 荧光恢复。这些发现为检测 AChE 活性提供了一种新方法。该测定法的检测限低至 0.05mU·mL 的 AChE。它具有高度选择性，其他酶没有明显干扰。它被应用于（加标）人血清中 AChE 活性的测定，以及（加标）湖水样品中 AChE 抑制剂的测定。
首次报道了通过控制聚多巴胺的合成来高灵敏度和选择性地检测 AChE 活性。
