Protein cage structures are ubiquitous in nature and present useful nanomaterials for applications ranging from drug delivery to the construction of nanoelectronics. Among protein cages, virus-like particles (VLPs), which are derived from the protein shell or capsid of viruses but lack pathogenic components, are particularly intriguing for constructing nanomaterials due to their stability, well studied molecular assembly and structures, which are often characterized to the molecular level. The VLP derived from the HK97 bacteriophage is a unique VLP; it self assembles from 420 copies of a single coat protein into a 60 nm spherical particle that forms a catanene structure, whereby the coat protein mononers become covalently cross-linked during its maturation process forming the molecular equivalent of protein chain mail. This ability to form a structure with all components covalently cross-linked gives the capsid inherent stability that can be exploited to construct robust nanomaterials. The research presented will discuss our recent findings in the development of the HK97 VLP, which focuses on the encapsulation of foreign protein cargos and synthetic compounds on the VLP interior.

Developing the HK97 virus-like particle as a nanomaterial platform

255th National Meeting (2018)

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