TY  - JOUR
A1  - Lehnert, Michael
A1  - Gorbahn, Miriam
A1  - Rosin, Christopher
A1  - Klein, Marc
A1  - Köper, Ingo
A1  - Al-Nawas, Bilal
A1  - Knoll, Wolfgang
A1  - Veith, Michael
T1  - Adsorption Conformation Behavior of Biotinylated Fibronectin on Streptavidin-Modified TiOx Surfaces Studied by SPR and AFM
T2  - Langmuir
N2  - It is well-known that protein-modified implant surfaces such as TiO2 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 TiOX 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 TiOX 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.
Y1  - 2011
UR  - https://whge.opus.hbz-nrw.de/frontdoor/index/index/docId/2826
SN  - 1520-5827
SN  - 0743-7463
VL  - 27
IS  - 12
SP  - 7743
EP  - 7751
PB  - ACS Publishing
CY  - Washnigton DC
ER  -