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Abstract
The work described in this thesis concerns the plasma polymers used for immobilization and adsorption of biomolecules. In particular, thin polymeric films bearing ether, anhydride, and amine functionalities were synthesis by plasma polymerization of these group containing monomers, i.e. di-(ethylene glycol) vinyl ether (EO2), maleic anhydride (MA), and
allylamine (AA). Additionally, the characterization of these films, their surface properties, and solution behavior were investigated in detail. Self-assembled monolayer (SAM) of octadecanethiol coated Au substrates were functionalized with different groups by plasma polymerization. The adsorption of the proteins fibrinogen, bovine serum, and immunoglobulin to these surfaces could be measured in situ by SPR spectroscopy. The results showed that protein adsorption was affected significantly by the different surface functional groups, and the polymerization conditions, as well as the thickness. Among three plasma polymer films, the affinity of proteins on PEO2 and PPAA is higher than that on PMA. The DNA immobilization behavior was found to be affected by the amine density and the buffer solution conditions. The data appear to suggest that the DNA oligonucleotides are able to penetrate into the low DC polymer network, thus reacting with functional groups deep within the polymer matrix, which does not seem to be possible with the highly cross-linked, high Peq films. A strong attraction between the longer chain DNA and the plasma polymer film was investigated by the pull-force curve using AFM. Also MM0, MM1 and MM2 are easily distinguished. Since PPAA is three-dimensional network in solution, DNA hybridization and dissociation is different from the two dimensional matrix.
