Theses and Dissertations at Montana State University (MSU)
Permanent URI for this collectionhttps://scholarworks.montana.edu/handle/1/733
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Item Chemical and biological properties of a phytotoxic glycopeptide from Corynebacterium insidiosum(Montana State University - Bozeman, College of Agriculture, 1971) Ries, Stephen MichaelItem Isolation and characterization of barley stripe mosaic virus protein(Montana State University - Bozeman, College of Agriculture, 1966) Gumpf, D. J.Item Protein cage architectures for targeted therapeutic and imaging agent delivery(Montana State University - Bozeman, College of Letters & Science, 2006) Flenniken, Michelle Lynne; Chairperson, Graduate Committee: Trevor Douglas; Mark Young (co-chair)Protein cage architectures such as viral capsids, heat shock proteins, and ferritins are naturally occurring spherical structures that are potentially useful nanoscale platforms for biomedical applications. This dissertation work demonstrates the utility of protein cages including their use as therapeutic and imaging agent delivery systems. Protein cage architectures have clearly demarcated exterior, interior, and interface surfaces and their structures are known to atomic level resolution. This information is essential for the engineering of functionalized nanoparticles via both chemical and genetic modification. In the process of tailoring protein cage architectures for particular applications, fundamental information about the architectures themselves is gained. The present work describes endeavors toward the use of three different protein cage architectures, the Cowpea chlorotic mottle viral capsid (CCMV), a small heat shock protein (Hsp) architecture originally isolated from the hyperthermophilic archaeon Methanococcus jannaschii, and human H-chain ferritin, as cell-specific therapeutic and imaging agent delivery systems. Each protein cage is roughly spherical, but their sizes differ; CCMV is 28 nm in diameter, whereas Hsp and HFn are 12 nm in diameter.