Adsorption and conformation behavior of biotinylated fibronectin on streptavidin-modified TiO(X) surfaces studied by SPR and AFM

© 2011 American Chemical Society

Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 27(2011), 12 vom: 21. Juni, Seite 7743-51
1. Verfasser: Lehnert, Michael (VerfasserIn)
Weitere Verfasser: Gorbahn, Miriam, Rosin, Christopher, Klein, Marcus, Köper, Ingo, Al-Nawas, Bilal, Knoll, Wolfgang, Veith, Michael
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2011
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Fibronectins titanium dioxide 15FIX9V2JP Biotin 6SO6U10H04 Streptavidin 9013-20-1 Titanium D1JT611TNE
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100 1 |a Lehnert, Michael  |e verfasserin  |4 aut 
245 1 0 |a Adsorption and conformation behavior of biotinylated fibronectin on streptavidin-modified TiO(X) surfaces studied by SPR and AFM 
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500 |a Date Revised 21.11.2013 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a © 2011 American Chemical Society 
520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Fibronectins  |2 NLM 
650 7 |a titanium dioxide  |2 NLM 
650 7 |a 15FIX9V2JP  |2 NLM 
650 7 |a Biotin  |2 NLM 
650 7 |a 6SO6U10H04  |2 NLM 
650 7 |a Streptavidin  |2 NLM 
650 7 |a 9013-20-1  |2 NLM 
650 7 |a Titanium  |2 NLM 
650 7 |a D1JT611TNE  |2 NLM 
700 1 |a Gorbahn, Miriam  |e verfasserin  |4 aut 
700 1 |a Rosin, Christopher  |e verfasserin  |4 aut 
700 1 |a Klein, Marcus  |e verfasserin  |4 aut 
700 1 |a Köper, Ingo  |e verfasserin  |4 aut 
700 1 |a Al-Nawas, Bilal  |e verfasserin  |4 aut 
700 1 |a Knoll, Wolfgang  |e verfasserin  |4 aut 
700 1 |a Veith, Michael  |e verfasserin  |4 aut 
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773 1 8 |g volume:27  |g year:2011  |g number:12  |g day:21  |g month:06  |g pages:7743-51 
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