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WIREs Nanomed Nanobiotechnol
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Highly ordered protein cage assemblies: A toolkit for new materials

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Abstract Protein capsids are specialized and versatile natural macromolecules with exceptional properties. Their homogenous, spherical, rod‐like or toroidal geometry, and spatially directed functionalities make them intriguing building blocks for self‐assembled nanostructures. High degrees of functionality and modifiability allow for their assembly via non‐covalent interactions, such as electrostatic and coordination bonding, enabling controlled self‐assembly into higher‐order structures. These assembly processes are sensitive to the molecules used and the surrounding conditions, making it possible to tune the chemical and physical properties of the resultant material and generate multifunctional and environmentally sensitive systems. These materials have numerous potential applications, including catalysis and drug delivery. This article is categorized under: Biology‐Inspired Nanomaterials > Protein and Virus‐Based Structures
Structural representation and dimensions of (a) horse spleen apoferritin (aFt) (1IER); (b) cowpea chlorotic mottle virus (CCMV) (1CWP); (c) tobacco mosaic virus (TMV) rod (3J06) and its two‐ring circular permutant (3KML); (d) M13 phage (1IFI); (e) stable protein 1 (SP1) (1TR0); (f) GroEL (1SS8); and (g) bovine mitochondrial peroxiredoxin (Prx) (1ZYE). Structures (not presented in scale) have been rendered with UCSF Chimera software V1.10.1, employing the structures deposited in the RCSB Protein Data Bank. The red color is indicative of local negative charge, but the coloring is not quantitative
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(a) Schematic representations of light‐sensitive dendrimers (top), an atomic force microscopy height image (bottom left), and a three‐dimensional (3D) representation (bottom right) of apoferritin (aFt) functionalized with ethyl orange. (b) Schematic representation of the phage‐display strategy for recognizing specific semiconductors, followed by nanoparticle (NP) synthesis by nucleation and subsequent organization in liquid crystals. (c) Surface deposition of phages in controlled patterns by the pulling method. (d) Liquid‐surface‐air profile of the phages, according to the ionic strength of the media. (e) Light‐absorbing properties of the deposited surfaces, according to thread diameter (Reprinted with permission from Koskela et al. (). Copyright 2014 American Chemical Society, Heo et al. (). Copyright 2019 Elsevier, Lee, Fan, et al. (). Copyright 2017 American Chemical Society, and Lee et al. (). Copyright 2002 Science)
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Protein cage crystals for catalysis. (a) Metal oxide nanoparticles (NPs) hosted inside ferritin crystals are accessible for a range of substrates and show oxidase‐like and peroxidase‐like catalytic activity. (b) Enzymes encapsulated inside viruses are catalytically active even when organized into three‐dimensional (3D) arrays. (c) Au atoms can be bound inside a ferritin cage and crystallized together with the cage. Crosslinking treatment of a single crystal enables structural characterization of the formation of a sub‐nanocluster via a reduction reaction (Reprinted with permission from Lach et al. (). Copyright 2017 Wiley Online Library, Uchida et al. (). Copyright 2018 American Chemical Society, and Maity et al. (). Copyright 2004 Wiley Online Library)
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Protein‐directed assembly. (a) Dendrimer size can be used to control the crystal lattice constant a. The dendrimer generation (G) and ionic strength [NaCl] present at the assembly affect crystal symmetry. (b) Self‐assembly of NP‐loaded ferritin cages yield highly ordered three‐dimensional (3D) superlattices. (c) Ring‐like proteins bind AuNPs through thiol‐anchoring points and induce anisotropic ligand distributions, which result in dipole formation. Multiple dipole–dipole interactions and thiol binding lead to stable AuNP chains (transmission electron micrograph (TEM) on right) (Reprinted with permission from Liljeström et al. (). Copyright 2015 American Chemical Society, Künzle et al. (). Copyright 2016 American Chemical Society, and Schreiber, Huber, Cölfen, and Schiller (). Copyright 2015 Nature)
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(a) Tobacco mosaic virus (TMV) and gold nanoparticles (AuNPs). Schematic (left) and cryo‐TEM images (middle) of the assemblies with an increasing number of AuNPs (scale bar = 50 nm) and a cryo‐electron tomographic (cryo‐ET) reconstruction of a superlattice wire with a right‐handed twist along the wire axis (right; scale bar = 200 nm). (b) GFP‐K72 with cowpea chlorotic mottle virus (CCMV) and apoferritin (aFt). A cryo‐TEM image of CCMV‐GFP‐K72 crystals with a schematic of CCMV packing (left) and amorphous aFt‐GFP‐K72 complexes (right), with a magnified image of the unoriented structure (right inset). (c) Cationic cyclophanes and aFt. Schematic of the studied hosts with the number of charges (top), the cryo‐TEM image of the aFT – P(10+) crystal viewed along the [110] projection axis (middle) with a fast Fourier transformation (FTT) of the crystal (middle inset) and an inverse and filtered FTT along the same projection axis (bottom left). A schematic of the crystal structure (bottom right). (d) Organic dyes and aFt. Schematic of the organic dyes (top) and optical microscopy images of aFt—phthalocyanine‐PTSA crystals at 20 mM NaCl (middle left; scale bar = 50 μm) and 30 mM NaCl solution (middle right) with a schematic of the aFt assemblies (bottom). (e) Optical disassembly of magnetoferritin complexes. Schematic (top) and transmission electron microscope (TEM) images (bottom) of free magnetoferritin self‐assembly with cationic dendrons and disassembly back to nanoparticles (NPs) after exposure to ultraviolet (UV) radiation (Reprinted with permission from Liljeström et al. (). Copyright 2017 Nature, Korpi et al. (). Copyright 2018 American Chemical Society, Beyeh et al. (). Copyright 2018 American Chemical Society, Mikkilä et al. (). Copyright 2016 American Chemical Society, and Kostiainen, Ceci, et al. (). Copyright 2011 American Chemical Society)
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(a) Schematic illustration of the assembly of apoferritin (aFt) with mutated 122 amino acid sites into face‐centered cubic (fcc) lattices by conventional crystallization or into body‐centered cubic (bcc) lattices by interaction between Zn coordination sites and ditopic linkers. (b) Schematic illustrations of binding modes of tetrahistidine‐modified tobacco mosaic virus (TMV) discs in the presence of metal cations into two‐dimensional (2D) assemblies. (c) Transmission electron microscope (TEM) and cryo‐TEM images of the 2D assemblies. Histidine‐modified stable protein 1 (SP1) (d; left) and peroxiredoxin (Prx) (e; left) in the presence of Ni‐NTA‐AuNPs, and corresponding TEM images showing the peapod structures (d and e; right). (f) GroEL carrying multiple spiropyran (SP) units and the reversible photochemical transformation. (g) Light‐mediated formation and dissociation of the nanotubular assembly (NT). (h) TEM images of the assembled (left) and monomeric (right) GroEL proteins (Reprinted with permission from Sontz et al. (). Copyright 2015 American Chemical Society, Zhang et al. (). Copyright 2018 American Chemical Society, Medalsy et al. (). Copyright 2008 American Chemical Society, Ardini et al. (). Copyright 2014 Royal Society of Chemistry, and Sendai et al. (2013). Copyright 2009 American Chemical Society)
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(a) Self‐assembly of stable protein 1 (SP1) into monodimensional stacks. Nanowire formed by the self‐assembly of SP1 (blue) and quantum dots (QDs) (yellow spheres). (b) Nanowire composed of SP1 rings (cyan) and core‐crosslinked micelles (CCMs) (yellow). (c) Assembly model of SP1 and a porphyrin‐containing PAMAM dendrimer (Reprinted with permission from Miao et al. (). Copyright 2014 American Chemical Society, Sun et al. (). Copyright 2015 American Chemical Society, and Sun et al. (). Copyright 2016 American Chemical Society)
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