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.

This book opens with a description of fundamental aspects of protein adsorption to surfaces, a phenomenon that plays a key role in biotechnological applications, especially at solid-liquid interfaces. Presented here are methods for studying adsorption kinetics and conformational changes such as optical waveguide lightmode spectroscopy (OWLS). Also described are sensitive bench techniques for measuring the orientation and structure of proteins at solid-liquid interfaces, including total internal reflection ellipsometry (TIRE), dual polarisation interferometry (DPI) and time of flight - secondary ion mass spectrometry (TOF–SIMS). A model study of fibronectin at polymer surfaces is included, as are studies using microporous membranes and textiles with immobilized enzymes for large-scale applications. Biocompatibility, anti-fouling properties and surface modification to modulate the adsorption and activity of biomolecules are among the other topics addressed in this invaluable book.

This book opens with a description of fundamental aspects of protein adsorption to surfaces, a phenomenon that plays a key role in biotechnological applications, especially at solid-liquid interfaces. Presented here are methods for studying adsorption kinetics and conformational changes such as optical waveguide lightmode spectroscopy (OWLS). Also described are sensitive bench techniques for measuring the orientation and structure of proteins at solid-liquid interfaces, including total internal reflection ellipsometry (TIRE), dual polarisation interferometry (DPI) and time of flight - secondary ion mass spectrometry (TOF–SIMS). A model study of fibronectin at polymer surfaces is included, as are studies using microporous membranes and textiles with immobilized enzymes for large-scale applications. Biocompatibility, anti-fouling properties and surface modification to modulate the adsorption and activity of biomolecules are among the other topics addressed in this invaluable book.

Proteins are exposed to various interfacial stresses during drug product development. They are subjected to air-liquid, liquid-solid, and, sometimes, liquid-liquid interfaces throughout the development cycle-from manufacturing of drug substances to storage and drug delivery. Unlike small molecule drugs, proteins are typically unstable at interfaces where, on adsorption, they often denature and form aggregates, resulting in loss of efficacy and potential immunogenicity. This book covers both the fundamental aspects of proteins at interfaces and the quantification of interfacial behaviors of proteins. Importantly, this book introduces the industrial aspects of protein instabilities at interfaces, including the processes that introduce new interfaces, evaluation of interfacial instabilities, and mitigation strategies. The audience that this book targets encompasses scientists in the pharmaceutical and biotech industry, as well as faculty and students from academia in the surface science, pharmaceutical, and medicinal chemistry areas.

This thesis describes a number of novel experiments contributing to the understanding of protein adsorption from both a fundamental and applied perspective. The first three papers involve the use of the localized surface plasmon resonance of gold nanospheres to measure protein conformational dependencies during heat and acid denaturation. A significant finding of all three studies is that the state and stability of BSA depends strongly upon local curvature. The last two papers investigate protein adsorption relevant to the biomaterial field. A unique fibril-like morphology is identified on galyfilcon A. Protein morphology is discussed in terms of bare lens morphology, roughness, and surface composition.