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.

Based on the March 1994 symposium sponsored by the Division of Colloid and Surface Chemistry at the 207th National Meeting held in San Diego, Calif. Contributions cover the theory and molecular mechanisms of protein adsorption (six papers); competitive adsorption of proteins (ten papers); the conformation and orientation of proteins at interfaces (seven papers); the effects of surface chemistry on protein adsorption (six papers); the role of adsorbed proteins in cell interactions with solid surfaces (four papers); and protein behavior at fluid-fluid interfaces (four papers). Some bandw photographs. Annotation copyright by Book News, Inc., Portland, OR

Purpose: To directly measure the quantity and degree of denaturation of biomaterial- adsorbed proteins over short time periods.

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.

Foams and froths are an important feature of everyday life; one only has to think of shaving foam, foam upholstery, fire fighting foam, bread, bear head, and ice cream. Less obvious but equally important are the foams and foaming processes which are being exploited in ever more complex and imaginative ways in industry. However, the unusual nature of foams, the fact that they are neither solids or liquids, and their very fragility has prevented scientists from obtaining a thorough understanding of even the basic principles of foam formation and stability. This volume presents papers on the physics, chemistry, structure and ultrastructure of foams by contributors from a wide range of backgrounds and research disciplines. The aim of the book is to present a unique multi-disciplinary cross section of work currently being undertaken on the subject of foams.

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.