Switching Peroxidase-Mimic Activity of Protein Stabilized Platinum Nanozymes by Sulfide Ions: Substrate Dependence, Mechanism, and Detection.

In the present work, we use β-casein as a model protein to prepare a smart β-casein stabilized Pt nanoparticle (CM-PtNP) with peroxidase mimicking activity and systematically investigate sulfide-mediated switching effect and mechanism of CM-PtNP nanozyme's activity. Sulfide-mediated activity switching effect depends heavily on the physicochemical properties of nanozymes and the identity of substrate. On one hand, the binding of sulfide to a Pt nanozyme surface leads to the transform from Pt2+ to Pt0, resulting in more active sites and the activity "switching on"; on the other hand, the binding of sulfide ions via Pt-S interaction blocks the active sites, resulting in the activity "switching off". For substrates 3,3',5,5'-tetramethylbenzidine and 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) diammonium salt, the two factors play different decisive roles since the interaction of substrate molecules with nanozyme allows their different distributions on nanozyme surfaces. By virtue of this specific response, excellent sulfide colorimetric sensors with different limits of detection were developed based on CM-PtNP with different substrates. This is the first report about a fundamental understanding of how substrates influence the anion-mediated activity switching effect by illuminating the nature of anion-nanozyme interaction and nanozyme-substrate interaction. This may be useful to rationally predict the environment factors on the activities of the nanozyme and to design an effective signal amplification based on target-induced nanozyme deactivation/activation.