Streptavidin‐coated surfaces suppress bacterial colonization 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 TiO 2 ‐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 TiO 2 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. © 2017 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 106A: 758–768, 2018.