The 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. / text
| Identifer | oai:union.ndltd.org:UTEXAS/oai:repositories.lib.utexas.edu:2152/25034 |
| Date | 07 July 2014 |
| Creators | Garland, Adam Till |
| Source Sets | University of Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis |
| Format | application/pdf |
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