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dc.contributor.authorRippner, Caitlin Marie Weiganden_US
dc.date.accessioned2013-05-15T08:00:43Z
dc.date.available2013-05-15T08:00:43Z
dc.date.issued2013-05-14en_US
dc.identifier.othervt_gsexam:1001en_US
dc.identifier.urihttp://hdl.handle.net/10919/22051
dc.description.abstractAmyloid aggregation involves the spontaneous formation of fibers from misfolded proteins. This process requires low energy input, results in robust fibers, and is thus of interest from a materials manufacturing perspective. The effect of glutamine content and hydrophobicity of template peptides on amyloid aggregation of a template-peptide system involving myoglobin was studied at near-physiological conditions by Fourier transform infrared spectroscopy, atomic force microscopy, field emission scanning electron microscopy, and nanoindentation. Hydrophobic interactions were found to be important for controlled hierarchical fiber growth via a cooperative mechanism, with the largest effect in myoglobin mixtures. Hydrophobic packing increased for most systems as aggregation progressed. The largest changes in structure occurred upon drying. When myoglobin was present with the highest glutamine-containing template (P7), the high glutamine peptide was not effective as a template, since it appeared to prefer self-catalysis. A low level of glutamine in some unordered templates was insufficient for amyloid development. However, templating was more important in glutamine-free templates mixed with myoglobin, which formed fibers with a surprisingly high elastic modulus. This may have been due to template patterning. Nanoindentation results confirmed that glutamine blocks were not necessary for strong intermolecular interactions and cooperative fibril formation.en_US
dc.format.mediumETDen_US
dc.publisherVirginia Techen_US
dc.rightsThis Item is protected by copyright and/or related rights. Some uses of this Item may be deemed fair and permitted by law even without permission from the rights holder(s), or the rights holder(s) may have licensed the work for use under certain conditions. For other uses you need to obtain permission from the rights holder(s).en_US
dc.subjectamyloiden_US
dc.subjectpeptideen_US
dc.subjectself-assemblyen_US
dc.subjectglutamine repeatsen_US
dc.subjectFTIRen_US
dc.subjectAFMen_US
dc.titleEffect of de novo peptide properties on self-assembling large amyloid fibersen_US
dc.typeThesisen_US
dc.contributor.departmentBiological Systems Engineeringen_US
dc.description.degreeMaster of Scienceen_US
thesis.degree.nameMaster of Scienceen_US
thesis.degree.levelmastersen_US
thesis.degree.grantorVirginia Polytechnic Institute and State Universityen_US
thesis.degree.disciplineBiological Systems Engineeringen_US
dc.contributor.committeechairBarone, Justin Roberten_US
dc.contributor.committeememberRenneckar, Scott Harolden_US
dc.contributor.committeememberZhang, Chenmingen_US


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