The behavior of proteins at solid-liquid interfaces
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.