Encapsulation of DNA‐Templated Chromophore Assemblies within Virus Protein Nanotubes

Escosura, Andrés de la; Janssen, Pim G. A.; Schenning, Albertus P. H. J.; Nolte, Roeland J. M.; Cornelissen, Jeroen J. L. M.

doi:10.1002/anie.201001702

Cited by 49 publications

(47 citation statements)

References 35 publications

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“…It turns out that the constituent protein can arrange into different morphologies depending on the guest molecules added. [11][12][13][14][15] This prompted us to study the solution behaviour of the CCMV and its capsid (with and without a synthetic polyelectrolyte present) at different pH values and salt concentrations, predominantly by scattering techniques.…”

Section: Introductionmentioning

confidence: 99%

Solution scattering studies on a virus capsid protein as a building block for nanoscale assemblies

et al. 2011

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Self-assembled protein cages are versatile building blocks in the construction of biomolecular nanostructures. Because of the defined assembly behaviour the cowpea chlorotic mottle virus (CCMV) protein is often used for such applications. Here we report a detailed solution scattering study of the CCMV virus and empty capsid. Contrast variation in small-angle neutron scattering (SANS) reveals a well-defined protein shell, with RNA associated mainly with its inner surface. The empty capsid has a protein shell with a diameter comparable to that of the virus, and has some weak scattering density associated on the inside, presumably the N-terminal part which is involved in RNA binding. Dynamic light scattering (DLS) and SANS show that the virus swells with increasing pH (5.0 to 7.5), whereas the empty capsid disassembles; the aggregation behaviour of the capsid protein becomes more complex at salt concentrations below 0.5 M NaCl. Incorporation of polystyrene sulfonate (PSS) in the capsid gives a particle with a solvent core, a polymer inner shell, and a protein outer shell, with a much smaller capsid outer diameter.

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Section: Introductionmentioning

confidence: 99%

Solution scattering studies on a virus capsid protein as a building block for nanoscale assemblies

et al. 2011

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“…This target is of course sensible as the porosity of the blood vessels in cancerous tumors allows particles to pass more efficiently. Since most globular VPs and VLPs are hollow and can readily assemble/dis‐assemble, they are just like many other protein cage structures, ideal to host small molecular, polymers, particles and even other proteins . It has to be noted that besides bioconjugation approaches, the covalent linking of bio‐active moieties to the interior or the exterior of the virus particle is also a common way to deliver payloads …”

Section: Virus Particles and Virus‐like Particles For Deliverymentioning

confidence: 99%

Viruses, Artificial Viruses and Virus‐Based Structures for Biomedical Applications

Rijn

Schirhagl

2016

Adv Healthcare Materials

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Nanobiomaterials such as virus particles and artificial virus particles offer tremendous opportunities to develop new biomedical applications such as drug- or gene-delivery, imaging and sensing but also improve understanding of biological mechanisms. Recent advances within the field of virus-based systems give insights in how to mimic viral structures and virus assembly processes as well as understanding biodistribution, cell/tissue targeting, controlled and triggered disassembly or release and circulation times. All these factors are of high importance for virus-based functional systems. This review illustrates advances in mimicking and enhancing or controlling these aspects to a high degree toward delivery and imaging applications.

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“…Stable guest cargo encapsulation in one environment and then efficient release in response to specific trigger is a research frontier and one of the hotspots in supramolecular chemistry, indicating promising applications in various fields such as drug/protein delivery, gene therapy, and so on . The nanoscale carriers arouse particular interest and attention due to the excellent permeability and retention properties, critically important in tumor treatment . The nanohosts are mainly designed via two principles, namely, the covalent conjugation of guest molecules and host carriers, or noncovalent encapsulation of cargo into nanoscale scaffolds .…”

Section: Introductionmentioning

confidence: 99%

Reversible Deactivation of Enzymes by Redox‐Responsive Nanogel Carriers

Peng

Rübsam

Jakob

et al. 2016

Macromol. Rapid Commun.

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Novel redox-responsive polymeric nanogels that allow highly efficient enzyme encapsulation and reversible modulation of enzyme activity are developed. The nanogel synthesis and encapsulation of enzyme are performed simultaneously via in situ crosslinking of pyridyldisulfide-functionalized water-soluble reactive copolymers, which are synthesized via reversible addition-fragmentation chain transfer copolymerization. Obtained nanogels with loaded cellulase demonstrate very good colloidal stability in aqueous solutions. The enzymatic activity of cellulase is greatly reduced when encapsulated in the nanogels and rapidly recovered in 10 × 10 m dithiothreitol solution. Fluorescence resonance energy transfer (FRET)-based experiments indicate that the recovered enzymatic activity is mainly ascribed to the release of the enzyme due to the degradation of the disulfide crosslinking network after addition of dithiothreitol (DTT), instead of the enhanced substrate transport rate. The developed enzyme immobilization method opens new possibilities for reversible activation/deactivation of enzymes and opens up new directions for targeted protein therapy and biotechnology applications.

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Encapsulation of DNA‐Templated Chromophore Assemblies within Virus Protein Nanotubes

Cited by 49 publications

References 35 publications

Solution scattering studies on a virus capsid protein as a building block for nanoscale assemblies

Solution scattering studies on a virus capsid protein as a building block for nanoscale assemblies

Viruses, Artificial Viruses and Virus‐Based Structures for Biomedical Applications

Reversible Deactivation of Enzymes by Redox‐Responsive Nanogel Carriers

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