Polystyrenes with carboxyl end-groups (PS-COOH)and poly (tert-butyl acrylates) (PtBA) of different molar mass were synthesised by anionic polymerisation using n-butyllithium as the initiator. Gel permeation chromatography (GPC) was used to calculate the molecular weight and polydispersity of these polymers. The tacticity of these polymers was determined using Carbon 13 Nuclear Magnetic Resonance Spectroscopy (13C NMR). FT-IR was used to confirm the tacticity of the samples. Matrix-assisted laser desorption ionisation time-of-flight mass spectrometry (MALDI-TOF) was used to confirm the presence of the carboxyl end-groups. All of the films studied in this project were transferred to mica substrates using the Langmuir-Blodgett deposition method. Both single layer and multiple layer films were constructed using this technique. Atomic force microscopy (AFM) was used to observe the surface topology of these films. / Doctor of Philosophy (PhD) (Science)

Adsorption kinetic data recorded for α-lactalbumin, β-casein, β-lactoglobulin, bovine serum albumin and lysozyme at silianized silica surfaces of low and high hydrophobicity, along with a simple model for adsorption and surfactant-mediated elution of protein, were used to analyze the removal of each protein by sodium dodecylsulfate (SDS) and dodecyltrimethylammonium bromide (DTAB) at each surface. The model relates resistance to surfactant elution to two rate constants: one governing conversion of removable protein to a nonremovable form (s₁), and one governing removal of protein by the surfactant (k [subscript s]). Elution of each protein from hydrophobic silica with SDS was interpreted as providing information relevant to protein-surface binding strength, or si; i.e., protein-specific differences in removal were a result of SDS adsorption to the surface and displacement of surface-bound protein, as opposed to solubilization driven by SDS binding to the protein. SDS-mediated removal of protein from surfaces of lower hydrophobicity were interpreted as generally proceeding according to a similar, displacement mechanism. The model indicated that data recorded for DTAB-mediated elution at each surface were generally less representative of protein-surface behavior, and more a function of k [subscript s], where differences in surfactant attachment to protein and solubilization appeared to play an important role in protein removal. Under controlled conditions use of the model would allow identification of cases where k [subscript s] in particularly protein specific, and illustrates the point that in such cases surfactant-mediated elution of a protein may reveal little about its surface behavior. / Graduation date: 1996

Graduation date: 1991

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Thesis (Ph. D.)--Lehigh University, 2000. / Includes bibliographical references and vita.

Thesis (Ph. D.)--University of Chicago, December 2003. / Includes bibliographical references. Also available on the Internet.

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