Construction of the Nickel Oxide Nanocoral Structure on Microscope Slides for Total Self-Assembly-Oriented Probe Immobilization and Signal Enhancement.

Abstract

Proper orientation of probes and the binding capacity of surfaces will determine the performance of bio-applications. It has been reported that immobilizing through bio-/chemical affinity is an efficient but gentle strategy to solve the above-mentioned issue. Herein, we introduce a total self-assembly approach via the strong affinity of nickel oxide (NiO) to the polyhistidine-tag (His-tag). It allows the efficient immobilizing His-tagged proteins with orientation. Furthermore, we find that the nanocoral structure can be formed after applying rapid thermal annealing at 1100 °C, which could increase the His-tagged protein binding capacity efficiently by the enhanced surface-to-volume ratio. Lastly, we demonstrate the NiO thin film with the nanocoral structure, which has great potential for universal biosensing with a wide range of biomolecules, including DNA, protein, and bacteria. Through His-tagged monomer streptavidin (His6-mSA) or His-tagged protein G (His6-protein G), the biotinylated DNA or antibody could be immobilized with proper orientation on the surface consequently to complete a sensitive biomolecule detection. Moreover, the NiO nanocoral structure has the advantages of high hydrophilicity, transmittance, and pH stability that are promising to develop into several kinds of bio-applications in the near future.