Elucidating the Thermodynamic Driving Forces of Polyanion-Templated Virus-like Particle Assembly.

A virus in its most simple form is comprised of a protein capsid that surrounds and protects the viral genome. The self-assembly of such structures, however, is a highly complex, multiprotein, multiinteraction process and has been a topic of study for a number of years. This self-assembly process is driven by the (mainly electrostatic) interaction between the capsid proteins (CPs) and the genome as well as by the protein-protein interactions, which primarily rely on hydrophobic interactions.

Experimental and Theoretical Determination of the pH inside the Confinement of a Virus-Like Particle.

In biology, a variety of highly ordered nanometer-size protein cages is found. Such structures find increasing application in, for example, vaccination, drug delivery, and catalysis. Understanding the physiochemical properties, particularly inside the confinement of a protein cage, helps to predict the behavior and properties of new materials based on such particles.

Nanoreactors via Encapsulation of Catalytic Gold Nanoparticles within Cowpea Chlorotic Mottle Virus Protein Cages.

Viral protein cage-based nanoreactors can be generated by encapsulation of catalytic metal nanoparticles within the capsid structure. In this method, coat proteins of the cowpea chlorotic mottle virus (CCMV) are used to sequester gold nanoparticles (Au NPs) in buffered solutions at neutral pH to form CCMV-Au hybrid nanoparticles. This chapter describes detailed methods for the encapsulation of Au NPs into CCMV protein cages.

Oligonucleotide Length-Dependent Formation of Virus-Like Particles.

Understanding the assembly pathway of viruses can contribute to creating monodisperse virus-based materials. In this study, the cowpea chlorotic mottle virus (CCMV) is used to determine the interactions between the capsid proteins of viruses and their cargo. The assembly of the capsid proteins in the presence of different lengths of short, single-stranded (ss) DNA is studied at neutral pH, at which the protein-protein interactions are weak.

Effect of Variations in Micropatterns and Surface Modulus on Marine Fouling of Engineering Polymers.

We report on the marine fouling and fouling release effects caused by variations of surface mechanical properties and microtopography of engineering polymers. Polymeric materials were covered with hierarchical micromolded topographical patterns inspired by the shell of the marine decapod crab Myomenippe hardwickii. These micropatterned surfaces were deployed in field static immersion tests.

Combining Protein Cages and Polymers: from Understanding Self-Assembly to Functional Materials.

Protein cages, such as viruses, are well-defined biological nanostructures which are highly symmetrical and monodisperse. They are found in various shapes and sizes and can encapsulate or template non-native materials. Furthermore, the proteins can be chemically or genetically modified giving them new properties.

Protein Cages as Containers for Gold Nanoparticles.

Abundant and highly diverse, viruses offer new scaffolds in nanotechnology for the encapsulation, organization, or even synthesis of novel materials. In this work the coat protein of the cowpea chlorotic mottle virus (CCMV) is used to encapsulate gold nanoparticles with different sizes and stabilizing ligands yielding stable particles in buffered solutions at neutral pH. The sizes of the virus-like particles correspond to T = 1, 2, and 3 Caspar-Klug icosahedral triangulation numbers.