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Medientyp: E-Artikel Titel: Streptavidin‐coated surfaces suppress bacterial colonization by inhibiting non‐specific protein adsorption Beteiligte: Ettelt, Volker; Ekat, Katharina; Kämmerer, Peer W.; Kreikemeyer, Bernd; Epple, Matthias; Veith, Michael Erschienen: Wiley, 2018 Erschienen in: Journal of Biomedical Materials Research Part A Sprache: Englisch DOI: 10.1002/jbm.a.36276 ISSN: 1549-3296; 1552-4965 Schlagwörter: Metals and Alloys ; Biomedical Engineering ; Biomaterials ; Ceramics and Composites Entstehung: Anmerkungen: Beschreibung: <jats:title>Abstract</jats:title><jats:p>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<jats:sub>2</jats:sub>‐surface to investigate its stability against proteolytic digestion and its suppression of initial bacterial adsorption of <jats:italic>Escherichia coli</jats:italic>, <jats:italic>Bacillus subtilis</jats:italic>, and <jats:italic>Streptococcus intermedius</jats:italic>. In contrast to nonmodified TiO<jats:sub>2</jats:sub> 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.</jats:p>