Electrostatic self-assembly of virus–polymer complexes

Kostiainen, Mauri A.; Hiekkataipale, Panu; Torre, Jose Á. de la; Nolte, Roeland J. M.; Cornelissen, Jeroen J. L. M.

doi:10.1039/c0jm02592e

Cited by 62 publications

(69 citation statements)

References 41 publications

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“…The multifunctional, and highly symmetric organization of subunits in the viral capsids provide for a unique environment for functional group display and modification 4–5 . Knowledge about the structure and assembly of virus capsids aids their use as powerful platforms for functional nanomaterials design and synthesis 6–12 . The assembly of repeating subunits into capsids generates highly monodisperse multivalent nanoparticles with distinct interior and exterior surfaces that can be used for encapsulation and/or display 13–14 .…”

Section: Introductionmentioning

confidence: 99%

Location of the Bacteriophage P22 Coat Protein C-Terminus Provides Opportunities for the Design of Capsid-Based Materials

et al. 2013

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Rational design of modifications to the interior and exterior surfaces of virus-like particles (VLPs) for future therapeutic and materials applications is based on structural information about the capsid. Existing cryo-electron microscopy based models suggest that the C-terminus of the bacteriophage P22 coat protein (CP) extends towards the capsid exterior. Our biochemical analysis through genetic manipulations of the C-terminus supports the model where the CP C-terminus is exposed on the exterior of the P22 capsid. Capsids displaying a 6xHis tag appended to the CP C-terminus bind to a Ni affinity column, and the addition of positively or negatively charged coiled coil peptides to the capsid results in association of these capsids upon mixing. Additionally, a single cysteine appended to the CP C-terminus results in the formation of intercapsid disulfide bonds and can serve as a site for chemical modifications. Thus, the C-terminus is a powerful location for multivalent display of peptides that facilitate nanoscale assembly and capsid modification.

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Section: Introductionmentioning

confidence: 99%

Location of the Bacteriophage P22 Coat Protein C-Terminus Provides Opportunities for the Design of Capsid-Based Materials

et al. 2013

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“…Future research will produce more of these biohybrid materials since new morphologies with new applications will emerge and the strength of combining electrostatic interactions with synthetic and biological structures is a straightforward and easy way of fabrication and allows also for large-scale fabrication under mild aqueous conditions. Not only for the directed intra-viral self-assembly but also for the directed aggregation of inter-viral assemblies where particles are directed by the surface charge and complementary charged polymers of different architectures and controlled/reversed by factors like ionic strength, pH or temperature [40].…”

Section: Artificial Assembly Of Virus Particlesmentioning

confidence: 99%

Polymer Directed Protein Assemblies

Rijn

2013

Polymers

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Protein aggregation and protein self-assembly is an important occurrence in natural systems, and is in some form or other dictated by biopolymers. Very obvious influences of biopolymers on protein assemblies are, e.g., virus particles. Viruses are a multi-protein assembly of which the morphology is dictated by poly-nucleotides namely RNA or DNA. This "biopolymer" directs the proteins and imposes limitations on the structure like the length or diameter of the particle. Not only do these bionanoparticles use polymer-directed self-assembly, also processes like amyloid formation are in a way a result of directed protein assembly by partial unfolded/misfolded biopolymers namely, polypeptides. The combination of proteins and synthetic polymers, inspired by the natural processes, are therefore regarded as a highly promising area of research. Directed protein assembly is versatile with respect to the possible interactions which brings together the protein and polymer, e.g., electrostatic, v.d. Waals forces or covalent conjugation, and possible combinations are numerous due to the large amounts of different polymers and proteins available. The protein-polymer interacting behavior and overall morphology is envisioned to aid in clarifying protein-protein interactions and are thought to entail some interesting new functions and properties which will ultimately lead to novel bio-hybrid materials.

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“…Crystallization is achieved through adjustment of the bathing conditions (salt and pH) to reduce or screen surface charges and resulting electrostatic repulsive forces and/or via the addition of precipitants such as PEG (Casselyn et al 2001). Alternative methods include the use of charged polymers, dendrimers, or dendrons to induce co-crystallization through electrostatic coupling between the additive (polymer or dendrimer/dendron structure) and the proteinacous nanoparticles with their patchy electrostatic pattern (Kostiainen et al 2011; Mikkilä et al 2013). …”

Section: Hierarchical Virus-based Assemblies—toward Metamaterialsmentioning

confidence: 99%

Photonics and plasmonics go viral: self-assembly of hierarchical metamaterials

Wen

Podgornik

Strangi

et al. 2015

Rend. Fis. Acc. Lincei

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Sizing and shaping of mesoscale architectures with nanoscale features is a key opportunity to produce the next generation of higher-performing products and at the same time unveil completely new phenomena. This review article discusses recent advances in the design of novel photonic and plasmonic structures using a biology-inspired design. The proteinaceous capsids from viruses have long been discovered as platform technologies enabling unique applications in nanotechnology, materials, bioengineering, and medicine. In the context of materials applications, the highly organized structures formed by viral capsid proteins provide a 3D scaffold for the precise placement of plasmon and gain materials. Based on their highly symmetrical structures, virus-based nanoparticles have a high propensity to self-assemble into higher-order crystalline structures, yielding hierarchical hybrid materials. Recent advances in the field have led to the development of virus-based light harvesting systems, plasmonic structures for application in high-performance metamaterials, binary nanoparticle lattices, and liquid crystalline arrays for sensing or display technologies. There is still much that could be explored in this area, and we foresee that this is only the beginning of great technological advances in virus-based materials for plasmonics and photonics applications.

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Electrostatic self-assembly of virus–polymer complexes

Cited by 62 publications

References 41 publications

Location of the Bacteriophage P22 Coat Protein C-Terminus Provides Opportunities for the Design of Capsid-Based Materials

Location of the Bacteriophage P22 Coat Protein C-Terminus Provides Opportunities for the Design of Capsid-Based Materials

Polymer Directed Protein Assemblies

Photonics and plasmonics go viral: self-assembly of hierarchical metamaterials

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