title: Orthogonal protein decoration of DNA nanostructures.
abstract: The development of robust DNA-protein coupling techniques is mandatory for applications of DNA nanostructures in biomedical diagnostics, fundamental biochemistry, and other fields in biomolecular nanosciences. The use of self-labeling fusion proteins, which are orthogonal to biotin-streptavidin and antibody-antigen interactions, is described for the site-selective protein decoration of two exemplary DNA nanostructures: a four-way junction X-tile motif and a 3D DNA tetrahedron. Multifunctional DNA superstructures bearing up to four different proteins are generated and characterized by electrophoresis and microplate-based functionality assays. Steric and electrostatic interactions are identified as critical parameters controlling the efficiency of DNA-protein ligation. The results indicate that this method is versatile and broadly applicable, not only for the functionalization of DNA architectures but also for the site-specific decoration of other molecular materials and devices containing several different proteins.
authors.affiliation: Technische Universität Dortmund, Fakultät Chemie, Biologisch-Chemische Mikrostrukturtechnik, Otto-Hahn Str. 6, D-44227 Dortmund.
authors.forename: Rebecca
authors.initials: R
authors.lastname: Meyer
authors.forename: Christof M
authors.initials: CM
authors.lastname: Niemeyer
mesh_terms: D004247:DNA / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D006147:Guanine / Q000737:chemistry; D006586:Hexanes / Q000737:chemistry; D006843:Hydrocarbons, Chlorinated / Q000737:chemistry; D049329:Nanostructures / Q000737:chemistry*; D059372:Nucleotide Motifs; D009841:Oligonucleotides / Q000737:chemistry; D011506:Proteins / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism
chemical_list: D006586:Hexanes; D006843:Hydrocarbons, Chlorinated; D009841:Oligonucleotides; D011506:Proteins; D011994:Recombinant Proteins; D006147:Guanine; D004247:DNA; C053283:1-chlorohexane