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Protein−DNA Double and Triple Layers:  Interaction of Biotinylated DNA Fragments with Solid Supported Streptavidin Layers

Authors :
Ijiro, K.
Ringsdorf, H.
Birch-Hirschfeld, E.
Hoffmann, S.
Schilken, U.
Strube, M.
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