Premium
Streptavidin‐coated surfaces suppress bacterial colonization by inhibiting non‐specific protein adsorption
Author(s) -
Ettelt Volker,
Ekat Katharina,
Kämmerer Peer W.,
Kreikemeyer Bernd,
Epple Matthias,
Veith Michael
Publication year - 2018
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.36276
Subject(s) - streptavidin , biotinylation , monolayer , adsorption , adhesion , materials science , protein adsorption , nanobiotechnology , biotin , proteolytic enzymes , biophysics , biochemistry , chemical engineering , nanotechnology , chemistry , enzyme , biology , nanoparticle , organic chemistry , engineering , composite material
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.