Developed an ALP probe that detects enzyme activity in bacteria using light activation, suggesting a new detection method.
Alkaline phosphatase (ALP) plays important biological roles for many living species, including bacteria. Here, we developed an ALP probe (CL-A1) using the dephosphorylation of an in situ light-activated chemiluminescent species based on a spiro-cyclobutane-substituted dioxetane scaffold. A sequential light-induced oxidation and ALP-mediated dephosphorylation of CL-A1 rapidly generated intense chemiluminescence (CL), which was stronger than that of the commercial CL substrates AMPPD and APS-5 tested in the presence of a signal enhancer. Analysis using Escherichia coli strains confirmed the applicability of CL-A1 for the sensitive detection of endogenous ALP activity using in situ light activation.
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Zhao et al. (2026) studied this question.
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