title: Adsorption and conformation behavior of biotinylated fibronectin on streptavidin-modified TiO(X) surfaces studied by SPR and AFM.
abstract: It is well-known that protein-modified implant surfaces such as TiO(2) show a higher bioconductivity. Fibronectin is a glycoprotein from the extracellular matrix (ECM) with a major role in cell adhesion. It can be applied on titanium oxide surfaces to accelerate implant integration. Not only the surface concentration but also the presentation of the protein plays an important role for the cellular response. We were able to show that TiO(X) surfaces modified with biotinylated fibronectin adsorbed on a streptavidin-silane self-assembly multilayer system are more effective regarding osteoblast adhesion than surfaces modified with nonspecifically bound fibronectin. The adsorption and conformation behavior of biotinylated and nonbiotinylated (native) fibronectin was studied by surface plasmon resonance (SPR) spectroscopy and atomic force microscopy (AFM). Imaging of the protein modification revealed that fibronectin adopts different conformations on nonmodified compared to streptavidin-modified TiO(X) surfaces. This conformational change of biotinylated fibronectin on the streptavidin monolayer delivers a fibronectin structure similar to the conformation inside the ECM and therefore explains the higher cell affinity for these surfaces.
authors: Laboratory of Biophysics, Physical Engineering Department, University of Applied Sciences of Gelsenkirchen, August-Schmidt-Ring 10, D-45665 Recklinghausen, Germany.
authors: Michael
authors: M
authors: Lehnert
authors: Miriam
authors: M
authors: Gorbahn
authors: Christopher
authors: C
authors: Rosin
authors: Marcus
authors: M
authors: Klein
authors: Ingo
authors: I
authors: Köper
authors: Bilal
authors: B
authors: Al-Nawas
authors: Wolfgang
authors: W
authors: Knoll
authors: Michael
authors: M
authors: Veith