Influence of various annealed Ni-Co nanowire properties upon the capability of immobilization of histidine-tagged protein

Ni-Co nanowire (NW) ligands, synthesized by TiO2 nanotube templates, were modified with annealing temperature to observe the immobilization of penta-histidine-tagged (5 x His-tagged) biotin. Protein microarrays, based on the theory of immobilized metal affinity chromatography (IMAC), were fabricated using the chelator of transition including Ni+2 and Co+2 metallic ions to capture the 5 x His-tagged biotin. One dimension of various annealing Ni-Co alloy NWs were analyzed for material characteristics and physical properties. Protein capture efficiencies were evaluated by measuring fluorescence intensities after dropping 5 x his-tagged biotin/streptavidin (5 x His-biotin/SA) on Ni-Co alloy NWs' grafted surfaces. It was observed that the higher saturation magnetization combined with lower electrical resistivity of metallic Ni-Co NW ligands may be useful for immobilizing 5 x His-tag biotins on solid surfaces to produce protein-functionalized surfaces. Due, not only to higher contact probability, but to the surface-to-volume ratio of the one dimension structure, the Ni-Co alloy NW ligand also proposes higher detected fluorescence sensitivity than that of Ni-Co film. (C) 2015 Elsevier B.V. All rights reserved.