Ferritin-catalyzed synthesis of ferrihydrite nanoparticles with high mimetic peroxidase activity for biomolecule detection

Abstract

Natural enzymes are generally sophisticated structural proteins that catalyze biological reactions with high specificity and efficiency and thus offer great potential in various disciplines, but intrinsic proteinic features such as easy denaturation and digestion restrict their practical application. So far, many functional nanomaterials with robust structures have been advanced as enzyme-mimetic catalysts to replace natural enzymes, however, their synthesis processes are generally complicated and require harsh experimental conditions such as high temperature and pressure. Herein, we report the facile synthesis of nanoparticles with high peroxidase-like activity by enzymatic catalysis. Specifically, by utilizing the intrinsic ferroxidase activity and mineralization capability of ferritin, ferrihydrite nanoparticles can be easily prepared within the apoferritin cavity at room temperature in aqueous solution (pH ∼ 7.0). Notably, reconstituted ferrihydrite nanoparticles exhibited comparative catalytic activity with a natural enzyme, horse radish peroxidase. Notably, when coupled with another oxidase, a dual-enzyme sensor system can be constructed for the detection of biomolecules such as glucose, and xanthine. Due to the biocompatibility and easy modification of the ferritin shell using well-established chemical and genetic techniques, the nanoparticles encapsulated by a protein shell possess great potential application in theranostics and immunoassays.