Adenosine-Related Compounds as an Enhancer for Peroxidase-Mimicking Activity of Nanomaterials: Application to Sensing of Heparin Level in Human Plasma and Total Sulfate Glycosaminoglycan Content in Synthetic Cerebrospinal Fluid.

A variety of compounds, such as DNA and protein, have been demonstrated to be effective in suppressing the catalytic activity of peroxidase-like nanomaterials. However, little investigations have been conducted to discover new chemical compounds for amplifying the catalytic activity of peroxidase-mimicking nanomaterials. This study discloses that adenosine analogues were useful as a universal enhancer for peroxidase-mimicking nanomaterials in the hydrogen peroxide-mediated oxidation of amplex ultrared at neutral pH. The optimal adenosine analogues for improving the peroxidase-like performance of citrate-stabilized gold nanoparticles (Au NPs), citrate-capped platinum NPs, bovine serum albumin-encapsulated gold nanoclusters, and unmodified magnetite NPs were found to be adenosine diphosphate (ADP), ADP, ADP, and adenosine monophosphate, respectively. The results show that adenosine analogue-induced enhancement in the peroxidase-like activity of nanomaterials was heavily associated with the number of adsorbed adenosine analogues onto the nanomaterial surface. The analysis of ADP-modified Au NPs by electron paramagnetic resonance spectroscopy indicates that the adsorbed ADP molecules on the Au NP surface not only activated HO but also strengthened the interaction between hydroxyl radicals and nanomaterials. By integrating the ADP-boosted catalytic activity of peroxidase-like Au NPs, surfen-triggered NP aggregation, and specific surfen-sulfated glycosaminoglycan (GAG) interaction, a turn-on fluorescent probe was constructed to quantify the heparin level in human plasma and total sulfate GAG content in synthetic cerebrospinal fluid.