The behavior of proteins at solid-liquid interfaces

dc.contributor.advisorAnslyn, Eric V., 1960-
dc.creatorGarland, Adam Tillen
dc.date.accessioned2014-07-07T16:17:28Zen
dc.date.issued2014-05en
dc.date.submittedMay 2014en
dc.date.updated2014-07-07T16:17:28Zen
dc.descriptiontexten
dc.description.abstractThe behavior of a protein molecule at the solid-liquid interface is a worthy scientific problem for at least three reasons. The main driving force for studying this problem is a practical one, as many areas of bio-related technologies, such as medical implants, biosensing, and drug delivery, require the understanding of protein-surface interactions. In this dissertation, the nature of the precursive weakly adsorbed state of proteins during binding is reviewed. From this perspective, the adsorption and binding of proteins to a solid block copolymer thin film was achieved with regular spacing. Further efforts produced a monolayer of green fluorescent protein (GFP) covalently bound with regular spacing and orientation to a diblock copolymer thin film. This protein could be folded and refolded by changing solvent characteristics. We also explored the binding of DC-SIGN to mannose and mannotriose bearing lipid membranes. While no binding was observed, the usefulness of the lipid-based glycan microarray was proven using the well-studied CTB-GM1 binding motif.en
dc.description.departmentChemistryen
dc.format.mimetypeapplication/pdfen
dc.identifier.urihttp://hdl.handle.net/2152/25034en
dc.language.isoenen
dc.subjectDiblock copolymeren
dc.subjectProtein adsorptionen
dc.subjectLipid bilayeren
dc.subjectDC-SIGNen
dc.titleThe behavior of proteins at solid-liquid interfacesen
dc.typeThesisen
thesis.degree.departmentChemistryen
thesis.degree.disciplineChemistryen
thesis.degree.grantorThe University of Texas at Austinen
thesis.degree.levelDoctoralen
thesis.degree.nameDoctor of Philosophyen
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