Phosphorylcholine (PC) based polymers have been used in medical devices to improve biocompatibility. In this study, PC based polymers were modified with either a cationic charge or combined with poly(butylmethacrylate) (PBMA) and their biocompatibility assessed through a series of biological assays. Protein adsorption assays revealed that the presence of a cationic charge significantly increased the number of proteins adsorbed. The total amount of protein adsorbed to PC with 30% cationic charge was considerably more then that adsorbed to the other samples. Fibronectin, albumin, complement factor B and immunoglobulins were found adsorbed to all samples. Clq however, was only adsorbed on samples containing 10% cationic charge or more. The presence of a cationic charge increased cell adhesion for both the fibroblast cells and the epithelial cells. Adhesion did not increase linearly with cationic charge, possibly due to alterations in protein adsorption, coating stability, and or cytotoxicity. Endothelial cells showed little to no cell adhesion on any of the PC cationic samples. Pre-coating materials in fibronectin increased endothelial cell adhesion, although this effect generally decreased as serum concentration increased. Pre-coating samples in laminin facilitated cell adhesion on PC with 20% cationic charge but not on PET or PC with 0% cationic charge. The combination of cationic charge and laminin may encourage cell adhesion, possibly through alterations in conformation of adsorbed proteins. Serum type affected adhesion and activation of mononuclear cells and granulocytes. The presence of a cationic charge increased the adhesion and activation of these two cell types. Adhesion and activation did not increase linearly with cationic charge, possibly due to differences in protein adsorption, coating stability and or cytotoxicity. The biocompatibility of PC and PBMA copolymer samples were assessed, looking at adhesion of corneal epithelial cells and macrophage cells. Adhesion of both of these cell these cell types increased as PBMA content increased and PC decreased. This is probably due to alterations in protein adsorption as a result of changes in surface hydrophobicity.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:405288 |
| Date | January 2002 |
| Creators | Long, Susanna |
| Publisher | University of Brighton |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
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