A novel alkaline phosphatase activity sensing strategy combining enhanced peroxidase-mimetic feature of sulfuration-engineered CoO with electrostatic aggregation.

Given alkaline phosphatase (ALP) takes part in the phosphorylation/dephosphorylation processes in the body, its activity is universally taken as an important indicator of many diseases, and thus developing reliable and efficient methods for ALP activity determination becomes quite important. Here, we propose a new sensing strategy for ALP activity by integrating the improved peroxidase-mimicking catalysis of sulfuration-engineered CoO with the hexametaphosphate ion (HMPi)-mediated electrostatic aggregation. After sulfuration engineering, the CoO composite coming from the pyrolysis of ZIF-67 exhibits enhanced peroxidase-mimetic catalytic ability to oxidize 3,3',5,5'-tetramethylbenzidine (TMB) to its oxide TMBox, offering a remarkable color change from colorless to mazarine; with the presence of HMPi, the rapid electrostatic assembly of negatively charged HMPi and positively charged TMBox leads to the aggregation of the latter, resulting in a color fading phenomenon; when ALP is added in advance to hydrolyze the HMPi mediator, the aggregation procedure is significantly suppressed, and such that the solution color can be recovered. Based on this principle, efficient determination of ALP activity was gained, giving a wide detection scope from 0.8 to 320 U/L and a detection limit as low as 0.38 U/L. Reliable analysis of the target in serum samples was also achieved, verifying the feasibility and practicability of our strategy in measuring ALP activity for clinical applications. Graphical abstract.