Ziyou Zhou

Colloidal Synthesis of Magnetic CuCr2S4 Nanocrystals and Nanoclusters

Nanocrystals and nanoclusters of the room-temperature magnetic spinel CuCr(2)S(4) have been synthesized using a facile solution-based method. The synthesis involves hot injection of an excess of 1-dodecanethiol (1-DDT) into a boiling coordinating solvent containing CuCl(2) and CrCl(3)·6H(2)O. Using octadecylamine (ODA) as a solvent yields cube-shaped nanocrystals with an average size of 20 ± 2 nm, while with oleylamine (OLA), nanoclusters with an average size of 31 ± 2.5 nm are obtained. In both cases, powder X-ray diffraction patterns confirmed the formation of the pure spinel phase without any impurities. While the synthesized powders are superparamagnetic near room temperature, they exhibit ferromagnetic behavior at lower temperatures, with magnetization (M(S)) values of 30 emu/g (1.63 μ(B)/f.u.) and 33 emu/g (1.79 μ(B)/f.u.) for the ODA- and OLA-capped nanocrystals and nanoclusters, respectively, at 5 K.

Directed self-assembly of CdS quantum dots on bacteriophage P22 coat protein?templates

The hierarchical organization of inorganic nanostructures has potential applications in diverse areas such as photocatalytic systems, composites, drug delivery and biomedicine. An attractive approach for this purpose is the use of biological organisms as templates since they often possess highly ordered arrays of protein molecules that can be genetically engineered for specific binding. Indeed, recent studies have shown that viruses can be used as versatile templates for the assembly of a variety of nanostructured materials because of their unique structural and chemical diversity. These highly ordered protein templates can be employed or adapted for specific binding interactions. Herein we report the directed self-assembly of independently synthesized 5 nm CdS nanocrystal quantum dots on ∼60 nm procapsid shells derived from wild-type P22 bacteriophage. The bacteriophage P22 shell is comprised of hexameric and pentameric clusters of subunits known as capsomeres. The pre-synthesized CdS QDs show the corresponding hexameric and pentameric patterns of assembly on these P22 shells, possibly by interacting with particular protein pockets.

Materials design using genetically engineered proteins

A variety of inorganic materials with amazingly complex structures and morphologies are produced by natural organisms. The fundamental mechanism underlying the natural biological synthesis of inorganic materials can be ascribed to the unique recognition and interaction of proteins with specific inorganic species. By mimicking natural biomineralization, genetically engineered proteins have in recent years been successfully utilized as platforms for the synthesis of inorganic nanostructures of various compositions under mild reaction conditions. Moreover, the precisely oriented assembly of genetically engineered proteins offers flexibility in designing inorganic nanostructures with desired complex architecture. This short review summarizes the recent progress in materials design using genetically engineered protein templates.

Formation mechanism of chalcogenide nanocrystals confined inside genetically engineered virus-like particles.

Engineered virus-like particles (VLP) are attractive for fabricating nanostructured materials for applications in diverse areas such as catalysis, drug delivery, biomedicine, composites, etc. Basic understanding of the interaction between the inorganic guest and biomolecular host is thus important for the controlled synthesis of inorganic nanoparticles inside VLP and rational assembly of ordered VLP-based hierarchical nanostructures. We have investigated in detail the formation mechanism and growth kinetics of semiconducting nanocrystals confined inside genetically engineered bacteriophage P22 VLP using semiconducting CdS as a prototypical example. The selective nucleation and growth of CdS at the engineered sites is found to be uniform during the early stage, followed by a more stochastic growth process. Furthermore, kinetic studies reveal that the presence of an engineered biotemplate helps in significantly retarding the reaction rate. These findings provide guidance for the controlled synthesis of a wide range of other inorganic materials confined inside VLP, and are of practical importance for the rational design of VLP-based hierarchical nanostuctures.

Selective Biotemplated Synthesis of TiO2 Inside a Protein Cage

Biological organisms have evolved tremendous control over the synthesis of inorganic materials in aqueous solutions at standard conditions. Such control over material properties is difficult to achieve with current synthesis strategies. Biotemplated synthesis of materials has been demonstrated to be efficient at facilitating the formation of various inorganic species. In this study, we employ a protein cage-based system to synthesize photoactive TiO2 nanoparticles less than 10 nm in diameter. We also demonstrate phase control over the material, with the ability to synthesize both anatase and rutile TiO2 using distinct biomineralization peptides within the protein cage. Finally, using analytical ultracentrifugation, we are able to resolve distinct reaction products and approximate their loading. We find that two distinct species comprise the reaction products, likely representing procapsid-like particles with early, precursor metal oxide clusters, and shells nearly full with crystalline TiO2 nanoparticles, respectively.

Pathways for Gold Nucleation and Growth over Protein Cages

Proteins are widely utilized as templates in biomimetic synthesis of gold nanocrystals. However, the role of proteins in mediating the pathways for gold nucleation and growth is not well understood, in part because of the lack of spatial resolution in probing the complicated biomimetic mineralization process. Self-assembled protein cages, with larger size and symmetry, can facilitate in the visualization of both biological and inorganic components. We have utilized bacteriophage P22 protein cages of ∼60 nm diameter for investigating the nucleation and growth of gold nanocrystals. By adding a gold precursor into the solution with preexisting protein cages and a reducing agent, gold nuclei/prenucleation clusters form in solution, which then locate and attach to specific binding sites on protein cages and further grow to form gold nanocrystals. By contrast, addition of the reducing agent into the solution with incubated gold precursor and protein cages leads to the formation of gold nuclei/prenucleation clusters both in solution and on the surface of protein cages that then grow into gold nanocrystals. Because of the presence of cysteine (Cys) with strong gold-binding affinity, gold nanocrystals tend to bind at specific sites of Cys, irrespective of the binding sites of gold ions. Analyzing the results obtained using these alternate routes provide important insights into the pathways of protein-mediated biomimetic nucleation of gold that challenge the importance of incubation, which is widely utilized in the biotemplated synthesis of inorganic nanocrystals.