Ni-Co nanowire (NW) ligands, synthesized by TiO2 nanotube templates, were modified with annealing temperature to observe the immobilization of penta-histidine-tagged (5 × 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 × 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 × his-tagged biotin/streptavidin (5 × 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 × 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.
All Science Journal Classification (ASJC) codes
- Mechanics of Materials
- Mechanical Engineering
- Metals and Alloys
- Materials Chemistry