Role of Surface Charge Density in Nanoparticle-Templated Assembly of Bromovirus Protein Cages
- 24 June 2010
- journal article
- research article
- Published by American Chemical Society (ACS) in ACS Nano
- Vol. 4 (7), 3853-3860
- https://doi.org/10.1021/nn1005073
Abstract
Self-assembling icosahedral protein cages have potencially useful physical and chemical characteristics for a variety of nanotechnology applications, ranging from therapeutic or diagnostic vectors to building blocks for hierarchical materials. For application-specific functional control of protein cage assemblies, a deeper understanding of the interaction between the protein cage and its payload is necessary. Protein-cage encapsulated nanoparticles, with their well-defined surface chemistry, allow for systematic control over key parameters of encapsulation such as the surface charge, hydrophobicity, and size. Independent control over these variables allows experimental testing of different assembly mechanism models. Previous studies done with Brome mosaic virus capsids and negatively charged gold nanoparticles indicated that the result of the self-assembly process depends on the diameter of the particle. However, in these experiments, the surface-ligand density was maintained at saturation levels, while the total charge and the radius of curvature remained coupled variables, making the interpretation of the observed dependence on the core size difficult. The current work furnishes evidence of a critical surface charge density for assembly through an analysis aimed at decoupling the surface charge and the core size.This publication has 45 references indexed in Scilit:
- A theory for viral capsid assembly around electrostatic coresThe Journal of Chemical Physics, 2009
- Self-assembly approaches to nanomaterial encapsulation in viral protein cagesJournal of Materials Chemistry, 2008
- Controlling viral capsid assembly with templatingPhysical Review E, 2008
- Packaging of a Polymer by a Viral Capsid: The Interplay between Polymer Length and Capsid SizeBiophysical Journal, 2008
- Core-like Particles of an Enveloped Animal Virus Can Self-Assemble Efficiently on Artificial TemplatesNano Letters, 2007
- Core-controlled polymorphism in virus-like particlesProceedings of the National Academy of Sciences of the United States of America, 2007
- Electrostatic origin of the genome packing in virusesProceedings of the National Academy of Sciences of the United States of America, 2006
- The cellular functions of clathrinCellular and Molecular Life Sciences, 2006
- EMAN: Semiautomated Software for High-Resolution Single-Particle ReconstructionsJournal of Structural Biology, 1999
- Quasi-equivalent viruses: a paradigm for protein assembliesJournal of Molecular Biology, 1997