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      S-layer-streptavidin fusion proteins as template for nanopatterned molecular arrays

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          Abstract

          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.

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          Most cited references21

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          Nanohedra: using symmetry to design self assembling protein cages, layers, crystals, and filaments.

          A general strategy is described for designing proteins that self assemble into large symmetrical nanomaterials, including molecular cages, filaments, layers, and porous materials. In this strategy, one molecule of protein A, which naturally forms a self-assembling oligomer, A(n), is fused rigidly to one molecule of protein B, which forms another self-assembling oligomer, B(m). The result is a fusion protein, A-B, which self assembles with other identical copies of itself into a designed nanohedral particle or material, (A-B)(p). The strategy is demonstrated through the design, production, and characterization of two fusion proteins: a 49-kDa protein designed to assemble into a cage approximately 15 nm across, and a 44-kDa protein designed to assemble into long filaments approximately 4 nm wide. The strategy opens a way to create a wide variety of potentially useful protein-based materials, some of which share similar features with natural biological assemblies.
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            Crystalline bacterial cell surface layers (s layers): from supramolecular cell structure to biomimetics and nanotechnology.

            An astonishingly broad application potential in biotechnology, biomimetics, and nanotechnology is revealed by studies on the structure, chemistry, biosynthesis, genetics, self-assembly, and function of supramolecular surface layers (S layers). These are monomolecular, crystalline assemblies of protein or glycoprotein subunits and represent one of the most commonly observed surface structures of prokaryotic cell envelopes (see schematic representation of an archaebacterial cell envelope). Copyright © 1999 WILEY-VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany.
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              Self-assembled nanostructures based on DNA: towards the development of nanobiotechnology.

              C Niemeyer (2000)
              DNA is a promising construction material for the supramolecular 'bottom-up' engineering of artificial nanostructured devices. The use of DNA for the selective positioning of macromolecular components, the fabrication of nanostructured DNA scaffolds, as well as the DNA-templated synthesis of nanometer-sized and mesoscopic complexes, consisting of inorganic and bioorganic compounds, are exciting areas of current research.
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                Author and article information

                Journal
                Proceedings of the National Academy of Sciences
                Proceedings of the National Academy of Sciences
                Proceedings of the National Academy of Sciences
                0027-8424
                1091-6490
                November 12 2002
                November 04 2002
                November 12 2002
                : 99
                : 23
                : 14646-14651
                Article
                10.1073/pnas.232299399
                137473
                12417763
                5c8fe5d5-7826-4485-8dd3-c8c6ef41ce91
                © 2002
                Product
                Self URI (article page): http://www.pnas.org/cgi/doi/10.1073/pnas.232299399

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