Nature offers a vast array of biological building blocks that can be combined with synthetic materials to generate a variety of hierarchical architectures. Viruses are particularly interesting in this respect because of their structure and the possibility of them functioning as scaffolds for the preparation of new biohybrid materials. We report here that cowpea chlorotic mottle virus particles can be assembled into well-defined micrometre-sized objects and then reconverted into individual viruses by application of a short optical stimulus. Assembly is achieved using photosensitive dendrons that bind on the virus surface through multivalent interactions and then act as a molecular glue between the virus particles. Optical triggering induces the controlled decomposition and charge switching of dendrons, which results in the loss of multivalent interactions and the release of virus particles. We demonstrate that the method is not limited to the virus particles alone, but can also be applied to other functional protein cages such as magnetoferritin.
Highly symmetrical protein cage architectures from three different iron storage proteins, heavy and light human ferritin chains (HuHFt and HuLFt) and ferritin from the hyperthemophilic bacterium Pyrococcus furiosus (PfFt), have been used as models for understanding the molecular basis of silver ion deposition and metal core formation inside the protein cavity. Biomineralization using protein cavities is an important issue for the fabrication of biometamaterials under mild synthetic conditions. Silver nanoparticles (AgNPs) were produced with high yields within PfFt but not within HuHFt and HuLFt. To explain the molecular basis of silver incorporation, the X-ray crystal structure of Ag-containing PfFt has been solved. This is the first structure of a silver containing ferritin reported to date, and it revealed the presence of specific binding and nucleation sites of Ag(I) that are not conserved in other ferritin templates. The AgNP encapsulated by PfFt were further characterized by the combined use of different physical-chemical techniques. These showed that the AgNPs are endowed with a narrow size distribution (2.1 +/- 0.4 nm), high stability in water solution at millimolar concentration, and high thermal stability. These properties make the AgNP obtained within PftFt exploitable for a range of applications, in fields as diverse as catalysis in water, preparation of metamaterials, and in vivo diagnosis and antibacterial or tumor therapy.
Protein cages such as ferritin and viral capsids are interesting building blocks for nanotechnology due to their monodisperse structure and ability to encapsulate various functional moieties. Here we show that recombinant ferritin protein cages encapsulating Fe(3)O(4)-γ-Fe(2)O(3) iron oxide (magnetoferritin) nanoparticles and photodegradable Newkome-type dendrons self-assemble into micrometer-sized complexes with a face-centered-cubic (fcc) superstructure and a lattice constant of 13.1 nm. The magnetic properties of the magnetoferritin particles are affected directly by the hierarchical organization. Magnetoferritin nanoparticles dispersed in water exhibit typical magnetism of single domain noninteracting nanoparticles; however, the same nanoparticles organized into fcc superstructures show clearly the effects of the altered magnetostatic (e.g., dipole-dipole) interactions by exhibiting, for example, different hysteresis of the field-dependent magnetization. The magnetoferritin-dendron assemblies can be efficiently disassembled by a short optical stimulus resulting in release of free magnetoferritin particles. After the triggered release the nanomagnetic properties of the pristine magnetoferritin nanoparticles are regained.
We report magnetic measurements on a macroscopic three-dimensional fcc array of iron-oxide nanoparticles. We observe typical nanomagnetism for the randomly packed configuration of nanoparticles, including dynamical freezing and superparamagnetism. By contrast, the nanoparticle "atoms" in the fcc configuration that form the crystal exhibit a low coercivity that is weakly temperature dependent with no superparamagnetism up to 400 K.
In this paper we report on the successful application of a protein crystallization technique to fabricate a three-dimensionally ordered array of magnetic nanoparticles, i.e. a novel type of metamaterial with unique magnetic properties. We utilize ferritin protein cages for the template-constrained growth of superparamagnetic nanoparticles of magnetite/maghemite Fe3O4-γ-Fe2O3 (magnetoferritin), followed by thorough nanoparticle bioprocessing and purification, and finally by protein crystallization. Protein crystallization is driven by the natural response of proteins to the supersaturation of the electrolyte, which leads to spontaneous nucleation and 3D crystal growth. Within a short period of time (hours to days) we were able to grow functional crystals on the meso-scale, with sizes of the order of tens, up to a few hundred micrometres. We present initial magnetic and Raman spectroscopy characterization results for the obtained 3D arrays of magnetic nanoparticles.
Self-organized Co/Pt nanoparticulate arrays offer a novel approach to fabricating magnetic recording media with the potential for supporting Terabit/in.2 recording densities. Protein-derived Co/Pt nanoparticles are prepared within apoferritin from aqueous reactants, with synthesis conditions controlling grain size, structure, and composition. Smooth films on glass disk substrates are produced by either spin coating or dip coating from aqueous dispersions of the precursor material. Films are typically annealed at 590 °C for 60 min with a 19 kPa (190 mBar) partial pressure of H2 to form the L10 phase. By varying the annealing conditions we are able to produce coercivities in the range of 500–8000 Oe. Electrical testing of Co/Pt nanoparticulate media using a contact test recorder shows that these nanoparticle films are capable of sustaining recording densities of more than 12.6 Gbits/in.2 (143.6 kfci, kilo flux changes per inch). In this article we will present results from finished films with regard to film structure, magnetic properties, and recording capabilities.
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