Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/27682
Title: Attaching proteins on modified silicon surfaces
Authors: DAI XUENI
Keywords: Lysozyme, Glucose oxidase, Protein adsorption, AFM, XPS, QCM
Issue Date: 10-Dec-2004
Source: DAI XUENI (2004-12-10). Attaching proteins on modified silicon surfaces. ScholarBank@NUS Repository.
Abstract: The adsorption behavior of Lysozyme (LSZ) onto alkyl-terminated Si (111) has been examined using QCM, XPS and AFM. The presence of adsorbed LSZ on the surface was detected by XPS. The kinetics study of the adsorption was monitored in situ by QCM. AFM studies revealed that the adsorption of LSZ is dominated by hydrophobic interactions and these interactions result in the rearrangement of LSZ clusters on the surface to form a LSZ layer with single-molecule thickness. The single-molecule layer elucidates that LSZ still retains its native structure despite experiencing strong hydrophobic interactions. The immobilization of glucose oxidase (GOX) onto amino-terminated Si (111) has been investigated combined XPS and AFM studies. AFM images revealed that it is suitable for immobilizing GOX employing cross-linking reaction. GOX molecules form rings like clusters in the first monolayer at different GOX concentrations. And protein height data have shown that the first layer is unfolded and denatured, which is due to the strong interactions between GOX and the surface.
URI: http://scholarbank.nus.edu.sg/handle/10635/27682
Appears in Collections:Master's Theses (Open)

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