Hall, Brenda;
(1990)
Interaction of blood components with polymers and biomimetic surfaces.
Doctoral thesis (Ph.D), UCL (University College London).
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Abstract
The work presented in this thesis describes the use of in vitro tests to monitor the blood compatibility of biomimetic surfaces. Phospholipids which predominate on the outer membrane surface of normal blood cells contain the phosphorylcholine polar head group. These surfaces are naturally non-thrombogenic. Phospholipids and polymers which contain the phosphorylcholine polar head group have been coated onto various substrates and analysed in terms of whole blood clot formation (as measured by the technique of Material Thrombelastography), protein adsorption, platelet and cellular interactions. Using Material Thrombelastography phospholipids which contain the phosphorylcholine group were found to limit the activation of clotting factors and reduce the rate and strength of clot formation in comparison to results obtained by negatively charged phospholipids. Furthermore, a polymerisable diacetylenic phospholipid and some polyesters which contain the phosphorylcholine group showed improved blood compatibility as compared to conventional materials. Phosphorylcholine lipids were also found to limit serum protein adsorption onto liposomes prepared from these lipids in contrast to negatively charged phospholipids. In particular dipalmitoylphosphatidylcholine was found to limit the adsorption of proteins (fibrinogen, -globulin and serum) onto polyethylene sheets coated with this lipid, and limit platelet and cellular surface interactions. Further studies have also been made to analyse polymer substrates which have been modified in order to covalently link phosphorylcholine groups to the surface. These results have been discussed in relation to the development of novel biomaterials which mimic natural biological membranes.
| Type: | Thesis (Doctoral) |
|---|---|
| Qualification: | Ph.D |
| Title: | Interaction of blood components with polymers and biomimetic surfaces. |
| Open access status: | An open access version is available from UCL Discovery |
| Language: | English |
| Additional information: | Thesis digitised by ProQuest. |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10116689 |
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