A virus-based biocatalyst (original) (raw)
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The assembly of individual molecules into hierarchical structures is a promising strategy for developing three-dimensional materials with properties arising from interaction between the individual building blocks. Virus capsids are elegant examples of biomolecular nanostructures, which are themselves hierarchically assembled from a limited number of protein subunits. Here, we demonstrate the bio-inspired modular construction of materials with two levels of hierarchy: the formation of catalytically active individual virus-like particles (VLPs) through directed self-assembly of capsid subunits with enzyme encapsulation, and the assembly of these VLP building blocks into three-dimensional arrays. The structure of the assembled arrays was successfully altered from an amorphous aggregate to an ordered structure, with a face-centered cubic lattice, by modifying the exterior surface of the VLP without changing its overall morphology, to modulate interparticle interactions. The assembly beh...
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Chemical Science, 2011
In the cell, enzymes are almost always spatially confined in crowded and tightly controlled cellular compartments. The entrapment of enzymes in artificial nanoreactors as biomimetic systems can be expected to contribute to the understanding of the activity and the interactions of enzymes in confined spaces. The capsid of the Cowpea Chlorotic Mottle virus (CCMV) represents such an artificial nanoreactor that can be used to encapsulate multiple proteins in its interior. Employing a controlled encapsulation process we are able to load a precise number of proteins (Pseudozyma antarctica lipase B and EGFP) into the CCMV capsid and to study their activity. In the case of the enzyme, our results indicate that the apparent overall reaction rate increases upon encapsulation and is almost independent of the number of enzymes in the capsid. These observation are the result of the extremely high confinement molarity of the enzyme inside the capsid (M conf ΒΌ $ 1 mM) leading to very rapid formation of the enzyme-substrate complex. These results highlight the importance of small volumes for efficient multi-enzyme cascade catalysis.
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Bottom-up self-assembly methods in which individual molecular components self-organize to form functional nanoscale patterns are of long-standing interest in the field of materials sciences. Such self-assembly processes are the hallmark of biology where complex macromolecules with defined functions assemble from smaller molecular components. In particular, plant virus-derived nanoparticles (PVNs) have drawn considerable attention for their unique self-assembly architectures and functionalities that can be harnessed to produce new materials for industrial and biomedical applications. In particular, PVNs provide simple systems to model and assemble nanoscale particles of uniform size and shape that can be modified through molecularly defined chemical and genetic alterations. Furthermore, PVNs bring the added potential to "farm" such bio-nanomaterials on an industrial scale, providing a renewable and environmentally sustainable means for the production of nano-materials. This...
Chemically induced self-assembly of enzyme nanorings
Methods in molecular biology (Clifton, N.J.), 2011
Continued exploration into the field of chemically induced dimerization (CID) has revealed a number of applications for its use in a broader context as a method of structural assembly (1-4). In particular, the use of CID technology to generate self-assembled (and selectively disassembled) protein toroids serves as a key advancement toward developing stable and controllable protein-based platforms. Such structures have broad application to the development of novel therapeutics, lab-on-a-chip technologies, and multi-enzyme assemblies (5, 6). This chapter describes a method of developing an enzymatically active protein nanostructure incorporating both a CID-based assembly region containing dihydrofolate reductase (DHFR) and an enzymatic region consisting of histidine triad nucleotide binding protein 1 (Hint1). Details of both the production and the characterization of this structure are provided.
Self-assembling of proteins and enzymes at nanoscale for biodevice applications
IEE Proceedings - Nanobiotechnology, 2004
Different nanotechnological strategies have been selected to implement biomolecular devices following a bottom-up or top-down approach depending on the biomolecule and on its functionality. Biomolecules have particular functionality and self-assembling capabilities that can be exploited for the implementation of both bioelectronic devices and multipurpose engineered biosurfaces. Surface preparation with supramolecular methods and microcontact printing have been developed and optimised to realise suitable functionalised surfaces. These surfaces can be used to link metalloproteins and enzymes for the implementation of nanobioelectronic devices and planar biosensors or to bind cells in order to promote their growth along predefined tracks and grooves. Some possible applications of these biosurfaces are shown and discussed. Results are presented for the realisation of a biomolecular nanodevice working in air based on the metalloprotein azurin immobilised in the solid state, the formation and characterisation of functional glutamate Dehydrogenase monolayers for nanobiosensing applications, the results of soft lithography processes on azurin for biosensor implementation, and the development of physiological self-assembled patterns of laminin-1 for cell culture applications and hybrid devices.
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Coordination Chemistry Reviews, 2011
New developments in the synthesis of nano-materials have opened new possibilities for creating and mastering nano-objects in order to design novel advanced catalytic materials. This concise conceptual review will give a glimpse into this fast growing research area discussing some of the possibilities in this direction, the perspectives and the gap to reduce to develop selective catalysts for complex multistep reactions. Emphasis is given to the opportunities offered by a tailored nano-design of the catalysts, from exploiting nano-confinement effects and supramolecular active sites synergies in nano-reactors to the new possibilities offered by new concepts such as the reduction of the relaxation time between two consecutive turnover cycles on a single active site and forcing a vectorial active site sequence in complex, multistep reactions. Other aspects discussed include the development of hierarchic pore structure to maximize catalyst effectiveness, metal complexes confined with solid cavities and the concept of nano-reactors, nanostructured composites and ordered 1D-type metal oxides. It is shown how significant progress in nano-materials has still not corresponded with progress in understanding the relationship between nanostructure and catalytic performance and the development of a more general strategy on the design of next-generation nano-catalysts.
Linker-Mediated Assembly of Virus-Like Particles into Ordered Arrays via Electrostatic Control
ACS Applied Bio Materials, 2019
Nanoscale virus-like particles (VLPs), that are themselves self-assembled from protein subunits, offer the possibility of generating hierarchicallyassembled functional materials such as biomimetic catalytic systems and optical metamaterials. We explore the capacity to control and tune higherorder assembly of VLPs into ordered array materials over a wide range of ionic conditions using a combination of experimental and computational methods. The integrated methodology demonstrates that P22 VLP variants, genetically engineered to exhibit different surface charges, selfassemble into ordered arrays in the presence of PAMAM dendrimers acting as oppositely charged, macromolecular linkers. Ordered assembly occurs at an optimal ionic strength that strongly correlates with the VLP surface charge. The ordered VLP arrays exhibit the same long-range order and a similar configuration of VLP-bound dendrimers, regardless of the VLP surface charge. The experimentally-validated model identifies key electrostatic and kinetic mechanisms underlying the self-assembly process, and guides the modulation of dendrimer concentration as a control parameter to tune the assembly of VLPs. The integrated approach opens new design and control strategies to fabricate active functional materials via the self-assembly of engineered VLPs.
An engineered virus as a scaffold for three-dimensional self-assembly on the nanoscale
Small (Weinheim an der Bergstrasse, Germany), 2005
Significant challenges exist in assembling and interconnecting the building blocks of a nanoscale device and being able to electronically address or measure responses at the molecular level. Self-assembly is one of the few practical strategies for making ensembles of nanostructures and will therefore be an essential part of nanotechnology. In order to generate complex structures through self-assembly, it is essential to develop methods by which different components in solution can come together in an ordered fashion. One approach to achieve ordered self-assembly on the nanoscale is to use biomolecules such as DNA as scaffolds for directed assembly because of the specificity and versatility they provide. Although several groups have demonstrated the usefulness of this approach, building ordered three-dimensional (3D) structures with DNA is difficult, because of the 1D nature of the scaffold. Using viruses as nanoscale scaffolds for devices offers the promise of exquisite control
Nano Letters, 2007
In this study, SP1, a ring-shaped highly stable homododecamer protein complex was utilized for the self-assembly of multiple domains in a predefined manner. Glucose oxidase (GOx) was fused in-frame to SP1 and expressed in Escherichia coli. Complexes where GOx encircled SP1 dodecamer were observed, and moreover, the enzymatic monomers self-assembled into active multienzyme nanotube particles containing hundreds of GOx molecules per tube. This work demonstrates the value of SP1 as a self-assembly scaffold.