Exploring Galvanic Replacement as a Method to Engineer Peroxidase-mimics Nanoparticles

Peroxidase enzymes are of critical importance within the scientific community for their applications in biosensing assays. In a living system, natural peroxidases function as catalysts in the oxidation of peroxide (e.g., H2O2) - a harmful byproduct of aerobic processes and convert them into harmless compounds. Such an ability allows peroxidases to serve as labels in biosensing assays, where they are conjugated to antibodies and accurately produce a detection signal by catalyzing substrates. However, due to intrinsic limitations, namely instability, Peroxidase made of proteins substantially inhibit broader applications. Alternatively, nanoparticles produced from noble metals have been found to exhibit peroxidase-like abilities and, therefore, can be used as synthetic enzymes with the potential to replace their natural counterparts. Given that the stability of most peroxidase mimics is already much better than their natural counterparts, in this field, the principal challenge has been creating substantial improvements to the catalytic efficiency of the mimics. This study sought to create a cage-like nanostructure ( denoted as nanocages) consisting of two platinum group metals. This experiment uses Galvanic replacement as a mechanism to hollow all Nanocages formed. Galvanic replacement has been primarily demonstrated using coinage metals ( Ex. Ag and Au). This experiment seeks to show that this process is viable for other Nobel metals, as well. In particular, palladium cubes were used as scaffolds or sacrificed templates to induce the reaction with a precursor containing a secondary Nobel metal (Platinum, Rhodium, or Ruthenium). Once viable samples where produced and checked via TEM ( Transmission Electron microscope), the peroxidase-like activity was compared to the activity of a non-hollowed nanostructure of the same material composition using TMB colorimetric assay