Enzymes are potent catalysts with high selectivity and specificity but are subject to instability due to temperature, hydrolytic activity by other enzymes, and reactive oxygen species. These drawbacks severely impede their utilization leading to a need for facile and effective immobilization techniques. Advancement in the synthesis of nanoparticles (NPs) with tunable size, controlled shape, and surface functionalization provides an excellent support for proteins. In this work hybrid supraparticles (SPs), self-assembled superstructures composed of proteins and inorganic nanoparticles, are formed as a tool for the encapsulation and immobilization of proteins, successfully separating them from the environments. SPs are formed by counterbalancing the underlying electrostatic repulsion and attractive interactions of proteins and NPs in the system. Here we show the spontaneous formation of five variations of hybrid SPs, self-assembled from proteins and NPs of various shapes. Iron disulfide (FeS<sub>2</sub>) NPs stabilized with thioglycolic acid (TGA), and zinc oxide (ZnO) NPs of various shapes (plates, spheres, and pyramids) were combined with protease, while cadmium telluride (CdTe) NPs stabilized with 2-(dimethylamino) ethanethiol (DMAET) were assembled with two proteins, cytochrome C (CytC) and formate dehydrogenase (FADH). A prominent feature of this work is to highlight the versatility of forming hybrid SPs, their stability in various environments, and potential application as a new class of nano-tools for a range of applications, specifically encapsulation. Experimental results show iron disulfide SPs are capable of encapsulating and releasing protein with no change in enzymatic activity. The properties of these newly fabricated SP assemblies make them an attractive tool to potentially aid in the development and understanding of complex biological systems.

Engineering supraparticle assemblies

2019 Spring National Meeting

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