Abstract
Prussian blue (PB) nanoparticles of intrinsic peroxidase and superoxide dismutase-like activities were prepared by the co-precipitation method and immobilized on amidine functionalized polystyrene latex (AL) particles. The interaction between the AL and PB particles and the colloidal stability of the resulting AL-PB hybrid composites were assessed at different mass ratios via determination of the charging and aggregation characteristics in the samples. The negatively charged PB nanoparticles strongly adsorbed on the oppositely charged AL particles resulting in a range of AL-PB composites of positive, neutral and negative overall charge, once the PB dose was increased. The AL-PB composite of a saturated PB layer on the surface of the AL particles formed considerably stable dispersions. Further, the morphology, structural and functional features of the AL-PB composites were explored by electron microscopy and enzymatic assays. The results revealed that the immobilization of PB nanoparticles not only provided a sustained catalytic surface but did not compromise the enzyme-like activities. The obtained stable composite is a promising agent in antioxidant therapies and wherever the aim is to reduce oxidative stress at laboratory or larger scales.
Highlights
Natural enzymes are remarkable catalysts under designated conditions, their production and purification is expensive and time-consuming [1]
The Prussian blue (PB) particles were prepared by the co-precipitation method [33] and the structure was confirmed by X-ray photoelectron spectroscopy (XPS) and spectrophotometry
The spectrum is characterized by a broad absorption band located at 700 nm, which is attributed to the charge transfer between Fe(II) and Fe(III) along Fe(II)–CN–Fe(III) confirming the successful synthesis of the desired PB
Summary
Natural enzymes are remarkable catalysts under designated conditions, their production and purification is expensive and time-consuming [1]. They suffer from inherent instability leading to a narrow window of operational conditions such as pH, pressure or temperature [2]. Nanomaterials of enzymatic function (so-called nanozymes) have been heavily explored as alternatives for native proteins due to their large surface area, high reactivity and tunable physico-chemical properties [3]. These nanozymes comprise a vast variety of nanostructures and enzymatic activities [4,5,6]
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