| Title | The effect of immobilization of thrombin inhibitors onto self-assembled monolayers on the adsorption and activity of thrombin |
| Publication Type | Journal Article |
| 2010 |
| Authors | Freitas, SC, Barbosa, MA, Martins, MCL |
| Journal | BiomaterialsBiomaterials |
| Volume | 31 |
| Issue | 14 |
| Pagination | 3772 - 3780 |
| Date Published | 2010/// |
| 01429612 (ISSN) |
| Absorption spectroscopy, Adsorption, adsorption kinetics, Albumins, Amino Acid Sequence, Amino acids, Angle measurement, article, Biomaterials, Blood, Blood clotting, Blood contact, Carbonyldiimidazole, Coagulation, Coagulation system, concentration (parameters), Concentration-dependent, Contact angle, D-phenylalanine, ellipsometry, Ethylene, Ethylene Glycol, ethylene glycol derivative, gold, Hemocompatibility, Humans, imidazole derivative, Immobilized Proteins, Infrared reflection absorption spectroscopy, infrared spectroscopy, Iodine Radioisotopes, isotope labeling, Medical Devices, monolayer culture, nanoanalysis, Nanostructured surface, peptide, Peptide immobilization, Peptides, phenylalanylprolylarginylprolylglycine, Phosphatases, priority journal, Protein adsorption, protein assembly, protein function, protein immobilization, quantitative study, Sams, Self assembled monolayers, Self-assembled monolayers, Serine protease, Solubility, Solutions, Spectroscopy, Fourier Transform Infrared, Surface functionalization, Surface Properties, Tetra, tetra(ethylene glycol), Thrombin, thrombin inhibitor, Thrombin inhibitors, Thrombus formation, unclassified drug, X ray photoelectron spectroscopy |
| Thrombus formation is the major problem associated with biomaterials for blood contact medical devices. The immobilization of inhibitors to thrombin, a serine protease that plays a central role on the coagulation system, on the surface of biomaterials should be a good strategy to avoid blood clotting and increase their hemocompatibility. The aim of this work is the design of a nanostructured surface with capacity to adsorb and inactivate thrombin. The pentapeptide sequence d-Phenylalanine-Proline-Arginine-Proline-Glycine (fPRPG), that was described as a thrombin inhibitor, was immobilized onto tetra(ethylene glycol) terminated self-assembled monolayers (EG4-SAMs). Surface containing different amounts of fPRPG were prepared using different concentrations of N,N′-Carbonyldiimidazole (CDI) during immobilization. The efficiency of fPRPG immobilization was followed using ellipsometry, contact angle measurements, Infrared reflection absorption spectroscopy (IRRAS) and X-ray photoelectron spectroscopy (XPS). Thrombin adsorption was quantified using radiolabelled thrombin and its activity in solution and after adsorption on the developed surfaces was assessed using a chromogenic assay. It was found that, although the immobilization of fPRPG on to EG4-SAMs does not increase its selectivity to thrombin, the activity of the adsorbed thrombin was inhibited in a peptide concentration dependent way. We concluded that SAMs with fPRPG immobilized in high amounts can be used as thrombin-inhibitor surfaces, which is a good step on the development of new surfaces for blood contact devices. © 2010 Elsevier Ltd. All rights reserved. |
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