Preparation of Barium-Hexaferrite/Gold Janus Nanoplatelets Using the Pickering Emulsion Method.

Janus particles, which have two surfaces exhibiting different properties, are promising candidates for various applications. For example, magneto-optic Janus particles could be used for in-vivo cancer imaging, drug delivery, and photothermal therapy. The preparation of such materials on a relatively large scale is challenging, especially if the Janus structure consists of a hard magnetic material like barium hexaferrite nanoplatelets. The focus of this study was to adopt the known Pickering emulsion, i.e., Granick's method, for the preparation of barium-hexaferrite/gold Janus nanoplatelets. The wax-in-water Pickering emulsions were stabilized with a combination of cetyltrimethyl ammonium bromide and barium hexaferrite nanoplatelets at 80 °C. Colloidosomes of solidified wax covered with the barium hexaferrite nanoplatelets formed after cooling the Pickering emulsions to room temperature. The formation and microstructure of the colloidosomes were thoroughly studied by optical and scanning electron microscopy. The process was optimized by various processing parameters, such as the composition of the emulsion system and the speed and time of emulsification. The colloidosomes with the highest surface coverage were used to prepare the Janus nanoplatelets by decorating the exposed surfaces of the barium hexaferrite nanoplatelets with gold nanospheres using mercaptan chemistry. Transmission electron microscopy was used to inspect the barium-hexaferrite/gold Janus nanoplatelets that were prepared for the first time.

Nanocomposites comprised of homogeneously dispersed magnetic iron-oxide nanoparticles and poly(methyl methacrylate).

Nanocomposites with a high, uniform loading of magnetic nanoparticles are very desirable for applications such as electromagnetic shielding and cancer treatment based on magnetically induced hyperthermia. In this study, a simple and scalable route for preparing nanocomposites with a high, uniform loading of magnetic nanoparticles is presented. The magnetic iron-oxide nanoparticles were functionalized with a methacrylate-based monomer that copolymerized in a toluene solution with the methyl methacrylate (MMA) monomer. The resulting suspension of magnetic nanoparticles decorated with poly(methyl methacrylate) (PMMA) chains in toluene were colloidal, even in the presence of a magnetic field gradient. Nanocomposites were precipitated from these suspensions. The transmission electron microscopy investigation of the prepared nanocomposites revealed that the magnetic nanoparticles were homogeneously dispersed in the PMMA matrix, even in amounts up to 53 wt %. The uniform dispersion of the nanoparticles in the PMMA matrix was attributed to the good solvation of the grafted PMMA chains from the magnetic nanoparticles by the PMMA chains of the matrix. The nanocomposites were superparamagnetic and exhibited large values for the saturation magnetization of up to 36 emu/g. Moreover, the nanocomposite with the largest amount of incorporated nanoparticles exhibited relatively large values for the specific power loss when subjected to alternating magnetic fields, giving this material great potential for the magnetically induced hyperthermia-based treatment of cancer.

Design of a single-chain polypeptide tetrahedron assembled from coiled-coil segments.

Protein structures evolved through a complex interplay of cooperative interactions, and it is still very challenging to design new protein folds de novo. Here we present a strategy to design self-assembling polypeptide nanostructured polyhedra based on modularization using orthogonal dimerizing segments. We designed and experimentally demonstrated the formation of the tetrahedron that self-assembles from a single polypeptide chain comprising 12 concatenated coiled coil-forming segments separated by flexible peptide hinges. The path of the polypeptide chain is guided by a defined order of segments that traverse each of the six edges of the tetrahedron exactly twice, forming coiled-coil dimers with their corresponding partners. The coincidence of the polypeptide termini in the same vertex is demonstrated by reconstituting a split fluorescent protein in the polypeptide with the correct tetrahedral topology. Polypeptides with a deleted or scrambled segment order fail to self-assemble correctly. This design platform provides a foundation for constructing new topological polypeptide folds based on the set of orthogonal interacting polypeptide segments.