Open AccessS-layer-streptavidin fusion proteins as template for nanopatterned molecular arrays
Author(s) -
Wulf-Dieter Moll,
Carina Huber,
Birgit Schlegel,
Dietmar Pum,
Uwe B. Sleytr,
Margit Sára
Publication year - 2002
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.232299399
Subject(s) - streptavidin , biotinylation , fusion protein , nanobiotechnology , fusion , liposome , chemistry , nanotechnology , biophysics , biotin , materials science , biochemistry , recombinant dna , biology , nanoparticle , linguistics , philosophy , gene
Biomolecular self-assembly can be used as a powerful tool for nanoscale engineering. In this paper, we describe the development of building blocks for nanobiotechnology, which are based on the fusion of streptavidin to a crystalline bacterial cell surface layer (S-layer) protein with the inherent ability to self-assemble into a monomolecular protein lattice. The fusion proteins and streptavidin were produced independently in Escherichia coli, isolated, and mixed to refold and purify heterotetramers of 1:3 stoichiometry. Self-assembled chimeric S-layers could be formed in suspension, on liposomes, on silicon wafers, and on accessory cell wall polymer containing cell wall fragments. The two-dimensional protein crystals displayed streptavidin in defined repetitive spacing, and they were capable of binding d-biotin and biotinylated proteins. Therefore, the chimeric S-layer can be used as a self-assembling nanopatterned molecular affinity matrix to arrange biotinylated compounds on a surface. In addition, it has application potential as a functional coat of liposomes.