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Adsorption Conformation Behavior of Biotinylated Fibronectin on Streptavidin-Modified TiOx Surfaces Studied by SPR and AFM

  • 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.

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Author:Michael Lehnert, Miriam Gorbahn, Christopher Rosin, Marc Klein, Ingo Köper, Bilal Al-Nawas, Wolfgang Knoll, Michael Veith
Parent Title (English):Langmuir
Publisher:ACS Publishing
Place of publication:Washnigton DC
Document Type:Article
Date of Publication (online):2018/09/10
Date of first Publication:2011/03/20
Publishing Institution:Westfälische Hochschule Gelsenkirchen Bocholt Recklinghausen
Release Date:2018/09/10
First Page:7743
Last Page:7751
Departments / faculties:Institute / Westfälisches Institut für Gesundheit
Licence (German):License LogoEs gilt das Urheberrechtsgesetz

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