Application of Peroxidase-Mimic Mn₂BPMP Boosted by ADP to Enzyme Cascade Assay for Glucose and Cholesterol

Abstract

The Mn2BPMP complex has an intrinsic peroxidase-like activity in the pH range of 5 to 8, especially a maximum activity at pH 7, while most peroxidase mimics operate at an acidic pH (mainly pH 4). Its peroxidase-like activity is high among small-molecule-based peroxidase mimics with a high reproducibility. In addition, we recently revealed that adenosine mono/diphosphate (AMP and ADP) significantly boosted the peroxidase-like activity of Mn2BPMP. These advantages imply that Mn2BPMP is suitable for biosensing as a substitute for horseradish peroxidase (HRP). Herein, we established a colorimetric one-pot assay system using the enzyme cascade reaction between analyte oxidase and ADP-boosted Mn2BPMP. The simple addition of ADP to the Mn2BPMP-based assay system caused a greater increase in absorbance for the same concentration of H2O2, which resulted in a higher sensitivity. It was applied to one-pot detection of glucose and cholesterol at 25 °C and pH 7.0 for a few minutes.

Keywords

• ADP-boosted peroxidase-like activity
• artificial peroxidase
• enzyme cascade assay