Berlin 2015 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 9: Biomaterials and Biopolymers I (joint BP/CPP)
BP 9.8: Vortrag
Montag, 16. März 2015, 16:30–16:45, EB 202
pH-dependent Ordered Fibrinogen Adsorption on Polyethylene Single Crystals — •Christian Helbing1, Robert Schulze1, Dominik Hering2, and Klaus D. Jandt1 — 1Chair of Materials Science (CMS), Otto-Schott-Institute of Materials Research (OSIM), Friedrich Schiller University Jena, Jena, Germany — 2Clemenshospital Münster, Münster, Germany
The biological performance of materials is mostly determined by protein adsorption at the biomaterials surface. Nanostructured surfaces can influence the assembly and orientation of adsorbed proteins. The aim of the current study was to control the protein adsorption by nanostructured surfaces. For this, we tested the hypothesis that human plasma fibrinogen (HPF) assemblies can be oriented on the (001) surface nanostructures of Polyethylene Single Crystals (PE-SC).
At a physiological pH of 7.4, HPF assemblies consisted of cross-linked HPF molecules, e.g., protofibrils, networks or sponge-like structures in dependence of the protein concentration. However, at an increased pH of 9.2 spherical-shaped and trinodal-shaped single HPF assemblies were observed. The observation of these multi protein assemblies (pH 7.4) and the single HPF assemblies (pH 9.2) can be explained by activated (pH 7,4) and deactivated (pH 9.2) HPFs αC-domains. While the single trinodal-shaped HPF molecules preferred an orientation along crystallographic [100] and [010] directions on the nanostructured PE-SC surface the HPF protofibrils showed no preferential orientation. The current study deepens the understanding of controlled protein assembly and orientation on nanostructured surfaces.