Enzyme-functionalized DNA nanostructures as tools for organizing and controlling enzymatic reactions
- PDF / 1,499,965 Bytes
- 5 Pages / 585 x 783 pts Page_size
- 68 Downloads / 209 Views
DNA-based scaffolds for the spatial confinement of enzymes The highly complex network of chemical reactions within the cell is mainly controlled through the confinement of enzymes into restricted spatial environments, such as on filaments, on biological membranes, and within organelles and other nanoscale compartments.1,2 In this way, high local concentrations of specific enzymes and signaling molecules in prescribed stoichiometric ratios can be realized to enhance reaction kinetics, substrates can be channeled through specific series of enzyme cascades (i.e., a sequence of successive activation reactions involving enzymes), and intermediates can be sequestered, thereby minimizing toxicity and competing cross reactions. In the effort to mimic such features, in vitro systems have been developed to immobilize enzymes with control over their spatial coordinates and dynamic temporal actuation (see Schulman and Simmel in this issue).3 A promising approach toward this goal uses DNA to construct ordered molecular assemblies, up to few hundreds of nanometers in size, with unique spatial addressability.4,5 This, together with the development of different chemical conjugation strategies to couple
proteins to nucleic acids (see Gothelf et al. in this issue),6 has now enabled the programmable organization of a distinct number of enzymes into linear arrays or small tile-tethered constructs onto two-dimensional (2D) DNA surfaces, or within small DNA confined volumes. Each of these strategies offers powerful opportunities for the design of functional nanomaterials that cannot be realized using any other nanoscale fabrication approach.
Oligonucleotide-tethered and small tiletethered enzymes The simplest way to explore proximity effects occurring in natural multienzyme complexes is to place distinct enzymes along a monodimensional scaffold and measure their activity as a function of their intermolecular distance. In this way, enzymatic reactions have been efficiently coupled,7 and the production of metabolic species has been increased (Figure 1a).8 Similarly, glucose oxidase enzymes have been modified with gold nanoparticles and scaffolded onto linear DNA molecules for the production of metallic nanoscale wires.9 In fact, the biocatalytic enlargement of gold nanoparticles via glucose
Guido Grossi, Interdisciplinary Nanoscience Center, Aarhus University, Denmark; [email protected] Andreas Jaekel, Center of Medical Biotechnology, Bionanotechnology Group, University of Duisburg-Essen, Germany; [email protected] Ebbe Sloth Andersen, Interdisciplinary Nanoscience Center, Aarhus University, Denmark; [email protected] Barbara Saccà, Center of Medical Biotechnology, Bionanotechnology Group, University of Duisburg-Essen, Germany; [email protected] doi:10.1557/mrs.2017.269
920
• VOLUME 42 • DECEMBER Bibliotheque 2017 • www.mrs.org/bulletin © 2017 Materials Research Downloaded MRS fromBULLETIN https://www.cambridge.org/core. de l'Universite Laval, on 18 Dec 2017 at 03:15:54, subject to the Cambridge Core terms of use, available at h
Data Loading...
