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Streptavidin-coated surfaces suppress bacterial colonisation by inhibiting non-specific protein adsorption

  • Streptavidin is a 58 kDa tetrameric protein with the highest known affinity to biotin with a wide range of applications in bionanotechnology and molecular biology. Dissolved streptavidin is stable at a broad range of temperature, pH, proteolytic enzymes and exhibits low non‐specific binding. In this study, a streptavidin monolayer was assembled directly on a biotinylated TiO2‐surface to investigate its stability against proteolytic digestion and its suppression of initial bacterial adsorption of Escherichia coli, Bacillus subtilis, and Streptococcus intermedius. In contrast to nonmodified TiO2 surfaces, streptavidin‐coated substrates showed only a negligible non‐specific protein adsorption at physiological protein concentrations as well as a significantly reduced bacterial adhesion. The antiadhesive properties were demonstrated to be the main reason for the suppression of bacterial adhesion, which makes this approach a promising option for future surface biofunctionalization applications.

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Author:Volker Ettelt, K. Ekkat, Peer W. Kämmerer, Bernd Kreikemeyer, Matthias Epple, Michael Veith
Parent Title (English):Journal of biomedical materials research : an official journal of The Society for Biomaterials, The Japanese Society for Biomaterials, and The Australian Society for Biomaterials. A
Publisher:New York
Place of publication:Wiley
Document Type:Article
Date of Publication (online):2018/07/12
Year of first Publication:2018
Publishing Institution:Westfälische Hochschule Gelsenkirchen Bocholt Recklinghausen
Release Date:2018/09/04
First Page:758
Last Page:768
Departments / faculties:Institute / Westfälisches Institut für Gesundheit
Licence (German):License LogoEs gilt das Urheberrechtsgesetz

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