COLL 185 |
| Kenyon McLane Evans and Mark H. Schoenfisch. Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3290 |
| The interfacial behavior of fibrinogen significantly impacts research in biomaterials and thrombosis. Neither the conformation nor biological behavior of fibrinogen adsorbed at solid surfaces is well understood. Herein, we report on the influence of surface substrate chemistry on the function of adsorbed fibrinogen. Fibrinogen adsorption and subsequent fibrin gel formation at several model interfaces is monitored with a quartz crystal microbalance and radiolabeling. Results indicate that fibrinogen adsorbs rapidly to hydrophobic and charged surfaces and initially assumes a rigid conformation. Notably, as adsorption proceeds to saturation, the viscoelasticity of the fibrinogen layer increases. In contrast, fibrinogen adsorption to hydrophilic surfaces proceeds more slowly and at a constant viscoelasticity. Differences in the underlying protein layer are shown to affect subsequent fibrin polymerization. While the initial fibrin gels formed at hydrophilic and hydrophobic substrates are similar, fibrin gel formed at hydrophobic surfaces becomes significantly more elastic as polymerization proceeds. |
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Adsorption of Macromolecules at Liquid-Solid Interfaces
Division of Colloid and Surface Chemistry |