Fabrication of a two-dimensional array of nano-particles using ferritin molecule
TL;DR: In this article, a two-dimensional array of iron-oxide loaded ferritin molecules formed by self-assembly at an air/water interface is transferred onto a hydrophobic Si surface and the protein shell of the Ferritin molecule is eliminated by 1 h heat-treatment at 500°C under nitrogen.
About: This article is published in Thin Solid Films.The article was published on 2001-08-01. It has received 290 citations till now.
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TL;DR: N nanoparticle-based immobilization of enzymes showed a broader working pH and temperature range and higher thermal stability than the native enzymes, and it is possible that co-immobilization of multi-enzymes could be achieved on these nanoparticles.
968 citations
TL;DR: In this paper, the salient aspects of self-assembly through the introduction of the recent challenges and breakthroughs in three categories: (i) types of selfassembly in bulk media; (ii) type of components for self-assembling in bulk medium; and (iii) selfassembly at interfaces.
708 citations
TL;DR: Hierarchical assembly of the functionalized cages paves the way for development of a new class of materials with a wide range of applications from electronics to biomedicine.
Abstract: Materials scientists increasingly draw inspiration from the study of how biological systems fabricate materials under mild synthetic conditions by using self-assembled macromolecular templates. Containerlike protein architectures such as viral capsids and ferritin are examples of such biological templates. These protein cages have three distinct interfaces that can be synthetically exploited: the interior, the exterior, and the interface between subunits. The subunits that comprise the building blocks of these structures can be modified both chemically and genetically in order to impart designed functionality to different surfaces of the cage. Therefore, the cages possess a great deal of synthetic flexibility, which allows for the introduction of multifunctionality in a single cage. In addition, hierarchical assembly of the functionalized cages paves the way for development of a new class of materials with a wide range of applications from electronics to biomedicine.
531 citations
TL;DR: Developments in the assembly of nanoparticles at liquid-liquid interfaces are reviewed where the assemblies can be controlled by tuning the size of the nanoparticles and the chemical characteristics of the ligands.
Abstract: Developments in the assembly of nanoparticles at liquid–liquid interfaces are reviewed where the assemblies can be controlled by tuning the size of the nanoparticles and the chemical characteristics of the ligands. Both synthetic and biological nanoparticles are discussed. By controlling the type of ligands, uniform and Janus-type nanoparticles can be produced where, at liquid–liquid interfaces, subsequent reactions of the ligands can be used to generate crosslinked sheets of nanoparticles at the interface that have applications including novel encapsulants, filtration devices with well-defined porosities, and controlled release materials. By controlling the size and volume fraction of the nanoparticles and the chemical nature of the ligands, nanoparticle–polymer composites can be generated where either enthalpy or entropy can be used to control the spatial distribution of the nanoparticles, thereby, producing auto-responsive materials that self-heal, self-corral assemblies of nanoparticles, or self-direct morphologies. Such systems hold great promise for generating novel optical, acoustic, electronic and magnetic materials.
511 citations
TL;DR: The present review discusses iron toxicity in plants with regard to plant growth and metabolism, metal interaction, iron-acquisition mechanisms, biofortification of iron, plant-iron homeostasis, gene function in crop improvement, and micronutrient interactions.
475 citations
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01 Jan 1963
TL;DR: In this paper, a sequence of procedures for identifying an unknown organic liquid using mass, NMR, IR, and UV spectroscopy is presented, along with specific examples of unknowns and their spectra.
Abstract: Presents a sequence of procedures for identifying an unknown organic liquid using mass, NMR, IR, and UV spectroscopy, along with specific examples of unknowns and their spectra,
11,753 citations
TL;DR: Transmission electron microscopy and electron diffraction analysis indicate that the entrapped mineral particles are discrete 6-nanometer spherical single crystals of the ferrimagnetic iron oxide magnetite (Fe3O4).
Abstract: The iron storage protein ferritin consists of a spherical polypeptide shell (apoferritin) surrounding a 6-nanometer inorganic core of the hydrated iron oxide ferrihydrite (5Fe2O3.9H2O). Previous studies have shown that the in vitro reconstitution of apoferritin yields mineral cores essentially identical to those of the native proteins. A magnetic mineral was synthesized within the nanodimensional cavity of horse spleen ferritin by the use of controlled reconstitution conditions. Transmission electron microscopy and electron diffraction analysis indicate that the entrapped mineral particles are discrete 6-nanometer spherical single crystals of the ferrimagnetic iron oxide magnetite (Fe3O4). The resulting magnetic protein, "magnetoferritin," could have uses in biomedical imaging, cell labeling, and separation procedures.
532 citations
TL;DR: The structure of horse spleen apoferritin, which has recently been refined, consists of 24 symmetrically related subunits forming a near-spherical hollow shell, and the protein influences both the rate of FeII-oxidation and the form of oxide produced.
Abstract: Although essential for most forms of life, too much iron is harmful. To cope with these antagonistic phenomena an iron-storage molecule, ferritin, has evolved. The structure of horse spleen apoferritin, which has recently been refined, consists of 24 symmetrically related subunits forming a near-spherical hollow shell. In ferritin the central cavity is occupied by an iron core of 'ferrihydrite', a geologically ephemeral mineral found in hot or cold springs and in mine workings, or produced in the laboratory by heating solutions of ferric salts. Ferritin itself forms most readily from apoferritin, in the presence of dioxygen, from FeII, not FeIII. Access to its interior is through small intersubunit channels, and the protein influences both the rate of FeII-oxidation and the form of oxide produced.
507 citations