Journal
CHEMICAL COMMUNICATIONS
Volume 57, Issue 74, Pages 9450-9453Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1cc03638f
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Funding
- Korea Institute of Ocean Science and Technology [PE99721]
- National Research Foundation of Korea (NRF) - Korea government (MSIT) [NRF-2020R1A2B5B01002392]
- Korea Institute of Marine Science & Technology Promotion (KIMST) [PE99721] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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We described an analyte-activatable artificial peroxidase system by caging a dimanganese complex with an analyte-reactive trigger. This system allowed adjustments of the detection target based on the trigger and detection modes, such as fluorescence and colorimetric. It was successfully applied to a versatile enzyme assay for leucine aminopeptidase and gamma-glutamyl transpeptidase based on spectrophotometric change induced from the oxidation of the peroxidase substrate by analyte-triggered peroxidase-like activity.
We described an analyte-activatable artificial peroxidase system (caged Mn-2(bpmp)) by caging a dimanganese complex, exhibiting peroxidase-like activity, with an analyte-reactive trigger. It allowed adjustments of the detection target to be applied depending on the trigger as well as the detection modes, such as fluorescence and colorimetric, as required. This system was successfully applied to a versatile enzyme assay for leucine aminopeptidase and gamma-glutamyl transpeptidase based on spectrophotometric change induced from the oxidation of the peroxidase substrate by analyte-triggered peroxidase-like activity.
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