| Title | Protein adsorption and clotting time of pHEMA hydrogels modified with C18 ligands to adsorb albumin selectively and reversibly |
| Publication Type | Journal Article |
| 2009 |
| Authors | Gonçalves, IC, Martins, MCL, Barbosa, MA, Ratner, BD |
| Journal | BiomaterialsBiomaterials |
| Volume | 30 |
| Issue | 29 |
| Pagination | 5541 - 5551 |
| Date Published | 2009/// |
| 01429612 (ISSN) |
| Adsorption, article, Biocompatible Materials, Biomaterials, blood clotting time, Blood Coagulation Tests, Body fluids, Clotting time, Coagulation, Coated Materials, Biocompatible, concentration response, controlled study, Fatty acids, fibrinogen, human serum albumin, hydrogel, Hydrogels, hydrophilicity, Ligands, long chain fatty acid, materials testing, Plasmas, PolyHEMA, Polyhydroxyethyl Methacrylate, polymacon, Polymer blends, polystyrene, Polystyrenes, priority journal, Protein adsorption, protein binding, Proteins, Serum Albumin, Surface modification, surface property, Surface treatment |
| This work intended to create a nanostructured biomaterial that would bind albumin in a selective and reversible way in order to inhibit the adsorption of other blood proteins and therefore minimize activation of coagulation. Different levels of C18 ligand have been immobilized on poly(2-hydroxyethyl methacrylate) (pHEMA). We hypothesize that samples with intermediate amounts of C18 ligand would allow albumin to recognize them and bind through its hydrophobic pockets specific for long chain fatty acids. Surface characterization has confirmed increasing amounts of C18 ligand on pHEMA as the percentage of C18 in solution increases, with maximum coverage achieved in 10% C18 samples. Adsorption from pure albumin solution revealed a small decrease in albumin adsorption from pHEMA to 1% C18 and 2.5% C18 samples, but on surfaces with 5% or higher C18 the amount of adsorbed albumin increased as the percentage of C18 increased. Competitive adsorption studies in the presence of both albumin and fibrinogen, and in the presence of all plasma proteins showed that 1% C18 and 2.5% C18 were the only surfaces selective for albumin, and that the presence of all plasma proteins may even potentiate albumin adsorption. Reversibility studies demonstrated that both 2.5% C18 and 5% C18 samples exchange 125I-albumin selectively in the presence of both unlabeled albumin and plasma, but 2.5% C18 samples presented higher exchangeability rates (58%). Clotting times using recalcified plasma revealed that samples with none or small amounts of C18 (pHEMA to 5% C18) did not shorten the clotting time compared to the negative control (polystyrene), indicating low activation of the intrinsic coagulation cascade. © 2009 Elsevier Ltd. All rights reserved.
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