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Protein−DNA Double and Triple Layers: Interaction of Biotinylated DNA Fragments with Solid Supported Streptavidin Layers
- Source :
- Langmuir; May 1998, Vol. 14 Issue: 10 p2796-2800, 5p
- Publication Year :
- 1998
-
Abstract
- The specific interaction of streptavidin with biotinylated lipids at the air−water interface leads to a formation of optically anisotropic two-dimensional streptavidin (2-D) crystals, where two of the original four biotin-binding sites remain free. These assembled streptavidin matrixes were used as a template for docking of double-stranded oligonucleotides biotinylated at a terminal or a centered position. A biotinylated lipid monolayer was deposited on an electrode of a quartz crystal microbalance (QCM), and docking processes of the protein and the oligonucleotides were detected as frequency changes related by mass changes on the QCM. The bis-biotinylated double-stranded oligonucleotides bound to the primary streptavidin layers made it possible to engineer protein−DNA−protein triple layers. Hydrolysis by a restriction endonuclease indicates that the biotinylated DNA bound to the streptavidin layers remains bioactive.
Details
- Language :
- English
- ISSN :
- 07437463 and 15205827
- Volume :
- 14
- Issue :
- 10
- Database :
- Supplemental Index
- Journal :
- Langmuir
- Publication Type :
- Periodical
- Accession number :
- ejs1138506