ANYL 152 |
| Virus-like particles (VLPs) are viruses in which the RNA core is removed and replaced with a nanoparticle. This example of engineered virus capsids and other protein cage structures have already shown promise as therapeutic and diagnostic vectors, imaging agents, and as scaffolds and microreactors for advanced nanomaterials synthesis. All these applications require the ability to control the interaction between the artificial core and the capsid proteins. One way to do this is to investigate the effect of the core size, shape, and surface chemistry on the assembly outcome. The viruses studied in our group are cowpea chlorotic mottle virus (CCMV) and brome mosaic virus (BMV). It has recently been demonstrated that varying the gold nanoparticle (GNP) core diameter provides control over the BMV capsid structure and that an optimum core size drives the VLPs to form nanoparticle-encapsulating capsids having a structure similar to the native virus. The assembly process is believed to be biased by interactions between an N-terminal domain of the capsid proteins and the nucleic acid. To support this, in vitro assembly using a mutant of CCMV lacking most of the N-terminal domain, ND34, showed the assembly of a variety of structural configurations. The present work seeks to investigate the importance of the role of the nanoparticle scaffold in assembly as compared with protein-protein interactions. To accomplish this, spherical and rod-shaped GNPs will be synthesized and encapsidated in CCMV and ND34 capsid proteins and the resulting VLP structures will be characterized and elucidated. The rod-shaped VLPs in particular, are unique in that they can serve as building blocks for 3D optical metamaterials. |
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Nanomaterials in Analytical Chemistry
1:25 PM-5:05 PM, Monday, April 7, 2008 Morial Convention Center -- Rm. 335, Oral
Division of Analytical Chemistry |