Font Size: a A A

Examination of protein adsorption with surface-sensitive spectroscopic techniques

Posted on:2004-12-22Degree:M.ScType:Thesis
University:University of Alberta (Canada)Candidate:Nsiah, FrancisFull Text:PDF
GTID:2461390011962895Subject:Chemistry
Abstract/Summary:
In this thesis, infrared reflection absorption spectroscopy (IRRAS) and surface plasmon resonance (SPR) imaging were employed to explore adsorption characteristics of human fibrinogen (HFG) human fibronectin (HFN), bovine serum albumin (BSA) and lysozyme (LYS).; Self-assembled monolayers (SAMs) on gold were used to control surface chemistry. The SAMs were characterized using IRRAS and contact angle measurements. Octadecanethiol (ODT) was used as a model neutral, hydrophobic surface. 16-mercapto-hexadecanoic acid (MHA) provides a hydrophilic, partially negatively charged surface at pH 7.4. CH2OH terminated monolayers of 11-mercapto-l-undecanol (MUL) was employed as a protein-resistant control surface. The differences in chemistries of the SAMs provided a platform to map variations in the amount of protein adsorbed and surface-induced protein conformation and/or orientation.; IRRAS was employed on single component monolayers to obtain information on surface coverage as well as on the adsorbed state of the proteins.; SPR imaging has been used for the first time as a means to visualized adsorbed state of proteins on patterned substrates. (Abstract shortened by UMI.)...
Keywords/Search Tags:Surface, Protein, IRRAS
Related items