TY - JOUR
T1 - Influence of various annealed Ni-Co nanowire properties upon the capability of immobilization of histidine-tagged protein
AU - Ho, Ching Yuan
AU - Lin, Tzu Hsuan
AU - Chang, Yaw Jen
N1 - Publisher Copyright:
© 2015 Published by Elsevier B.V.
PY - 2015/7/17
Y1 - 2015/7/17
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/84937468813
UR - https://www.scopus.com/pages/publications/84937468813#tab=citedBy
U2 - 10.1016/j.jallcom.2015.07.003
DO - 10.1016/j.jallcom.2015.07.003
M3 - Article
AN - SCOPUS:84937468813
SN - 0925-8388
VL - 648
SP - 726
EP - 731
JO - Journal of Alloys and Compounds
JF - Journal of Alloys and Compounds
ER -