Spectroscopic and calorimetric studies of aggregated macromolecules

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dc.contributor.advisorVanden Bout, David A.en
dc.creatorKitts, Catherine Carter, 1979-en
dc.date.accessioned2008-08-28T23:39:29Zen
dc.date.accessioned2017-05-11T22:18:12Z
dc.date.available2008-08-28T23:39:29Zen
dc.date.available2017-05-11T22:18:12Z
dc.date.issued2007en
dc.descriptiontexten
dc.description.abstractDifferent optical and calorimetric techniques were utilized to gain a better understanding of aggregated macromolecules. This research looked at two different macromolecules: poly(9,9'-dioctylfluorene), a conjugated polymer that forms aggregates in organic solvents; and bovine insulin, which forms amyloid fibrils. Conjugated polymers are of increasing interest due to their thermal stability and ease of solution processing for use in devices. A member of the polyfluorene family, poly(9,9'-dioctylfluorene) (PFO), has been studied due to its blue-emitting spectral properties. However, PFO has been found to form aggregates in solution, which is detected by the presence of a red-shifted absorption peak. This peak is caused when a section of the backbone planarizes forming the [beta]-phase. The [beta]-phase can be removed from the solution upon heating and will not return until the solution is cooled, making it a non-equilibrium process. The dissolution and reformation of the -phase were monitored using absorption spectroscopy and differential scanning calorimetry. Atomic force microscopy (AFM) and near-field scanning optical microscopy (NSOM) were able to probe the aggregates in films. It is important to understand polymer properties in solution in order to understand film morphology. Amyloid fibrils contribute to over 20 different neurodegenerative diseases, in which cures have yet to be found. The fibrils form when a soluble protein misfolds and self-assembles to form insoluble protein aggregates, and the cause of the fibril formation in vivo has still yet to be determined. Spectroscopy studies have been made possible with the use of fluorescent dyes: thioflavin T (ThT), BTA-2, and Congo red (CR). These dyes bind to amyloid fibrils and exhibit changes in their spectral properties. However, the exact mechanism for the binding of these dyes has only recently been studied. Through the use of calorimetry, the forces involved with binding of ThT and CR to amyloid fibrils can be determined. Absorption and fluorescence spectroscopy techniques were employed to study the spectral properties of these dyes. Polarized NSOM was used to determine the ThT or BTA-2's orientation with an individual fibril. Understanding how these dyes bind to fibrils will enable researchers to use spectroscopy to study the early stages of fibril formation.en
dc.description.departmentChemistry and Biochemistryen
dc.description.departmentChemistryen
dc.format.mediumelectronicen
dc.identifierb68900491en
dc.identifier.oclc174284516en
dc.identifier.urihttp://hdl.handle.net/2152/3296en
dc.language.isoengen
dc.rightsCopyright is held by the author. Presentation of this material on the Libraries' web site by University Libraries, The University of Texas at Austin was made possible under a limited license grant from the author who has retained all copyrights in the works.en
dc.subject.lcshConjugated polymersen
dc.subject.lcshConjugated polymers--Spectraen
dc.subject.lcshAmyloiden
dc.subject.lcshInsulinen
dc.subject.lcshFluorescence spectroscopyen
dc.subject.lcshCalorimetryen
dc.subject.lcshScanning probe microscopyen
dc.subject.lcshFluorescence microscopyen
dc.titleSpectroscopic and calorimetric studies of aggregated macromoleculesen
dc.type.genreThesisen

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