Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.669567
Title: Toward high throughput screening of assembly-optimised ferritin nanocage libraries applied to nanotechnology
Author: Cornell, Thomas Andrew
ISNI:       0000 0004 5369 128X
Awarding Body: King's College London (University of London)
Current Institution: King's College London (University of London)
Date of Award: 2015
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Abstract:
Protein nanocages have been directed toward a myriad of applications such as drug delivery and material science as well as model systems to study protein folding and self-assembly. These pursuits, because they have conventionally been explored through often indirect techniques which typically are implemented in a protracted and high-resource intensive manner, have been limited by the inability to design rapidly novel and unique properties of these proteins or to discover conditions most ideal for their efficacy. This thesis describes experiments performed to explore protein nanocage applications and fundamental self-assembly in a traditional sense while providing a path for the broadening of these goals by developing a novel technique to explore the properties and conditions of nanocage assembly quickly and directly. Chapter 1 provides an introduction to protein quaternary structure and nanocage assembly with a focus on the ferritin family of proteins. Chapter 2 describes the attempt to apply protein nanocages to nanotechnology. Chapter 3 reports the application of x-ray crystallography to understand the role of sub-tertiary structure in the generation of protein nanocage quaternary structure. However, although this work advanced nanoscience and provided fundamental insight, it became evident that these strategies could be augmented through the development of a more rapid screening technique for protein cage assembly. Thus, Chapter 4 and Chapter 5 develop this technique with two different protein nanocages in vitro, while Chapter 6 further expands it to allow the high throughput screening of protein libraries in vivo. This method could help to expand and hasten our understanding of protein quaternary structure as well as to facilitate the development or enhancement of nanocage applications where tailored properties would be desired for the generation of size selective nanoparticles or for the transport and delivery of drugs.
Supervisor: Orner, Brendan Patrick; Sutton, Brian John Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.669567  DOI: Not available
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