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Contribution (Oral)
SUPEROXIDE DISMUTASE CONJUGATED TO NANOPATTERN SURFACES: IMMOBILIZATION
OF ENZYME IN NANOSTRUCTURE MATERIALS FOR BIOSENSOR APPLICATIONS.
Aaron C. Asensio1, Edurne Teiletxea Malda1,2, Iñaki Cornago1, Jose F. Moran2
1FideNa,
2Instituto
Centro Jerónimo de Ayanz, C/ Tajonar s/n, E-31006 Pamplona, Navarra, Spain
de Agrobiotecnología, Universidad Pública de Navarra-CSIC-Gobierno de Navarra, Campus
de Arrosadia s/n, E-31006, Pamplona, Navarra, Spain
[email protected]
Design and development of devices based on biomolecule immobilization onto nanopatterned surfaces
are of great interest in the field of bio-nanotechnology, mainly due to its potential applications in the
fields of biosensors, disease diagnosis, and optimization of enzymatic or catalytic processes. Also,
nanopatterned surfaces with different motives may be fabricated to bind biomolecules in a predetermined way. The designed nanopattern may provide an improved functionality for the catalytic
properties or for the detection of the assembled proteins and their ligands.
Superoxide dismutases are enzymes that catalyze the dismutation of superoxide into oxygen and
hydrogen peroxide. These enzymes have great physiological significance and therapeutic potential in
the prevention of the oxidative damage from superoxide radicals, and may serve to estimate
peroxynitrite radicals [1]. The superoxide radical and SOD have been implicated in many disease states
including inflammatory diseases, diseases of ischemia and reperfusion, neurodegenerative diseases,
and cancer, as well as more subtle roles in cell signaling and perhaps in immune function [2]. FeSOD, a
plant superoxide dismutase, is a very stable biomolecule, it contains an iron atom in a well
characterized 3D protein structure [3], which may serve as model for conjugates studies, as well as a
model for develop methods and strategies easily applicable to human SODs.
In this work, we present the characterization of the conjugates between FeSOD enzyme and
nanopatterned surfaces. We will describe the manufacturing of the nanopatterned surfaces, the
production and purification of recombinant protein FeSOD, the functional immobilization of the purified
enzymes, as well as the results of the immunological and enzymatic methods, used for demonstrate the
protein is effectively attached to the nanostructure and maintains intact its activity.
Acknowledgements
We gratefully acknowledge FideNa, the Public University of Navarra (OTRI 2010 800 156) and the
Government of Navarra, Department of Innovation, Business and Employment, for its financial support
under SABioD project (IIQ14076.R1).
References
[1] Larrainzar, E., Urarte, E., Auzmendi, I., Ariz, I., Arrese-Igor, C., González, E.M., Moran, J.F.,
Methods in Enzymology, 437 (2008) 605.
[2] McCord, J.M. and Edeas M.A. Biomedicine & Pharmacotherapy, 59 (2005) 139.
[3] Muñoz, I.G., Moran, J.F., Becana, M., Montoya, G. Acta Crystallographica - Section D Biological
Crystallography, 59 (2003) 1070.
Contribution (Oral)
Figure 1
Left: Nanopatterned gold lines over silica surface. Right: Detection of the FeSOD attached over the nanostructured
surface by using antibodies conjugated with Cy2 fluorophore.