TY - JOUR
T1 - Crystallographic structure of Ni-Co coating on the affinity adsorption of histidine-tagged protein
AU - Chang, Yaw Jen
AU - Chen, Sheng Zheng
AU - Ho, Ching Yuan
N1 - Funding Information:
This work was supported by the Ministry of Science and Technology (MOST) of Taiwan, R.O.C. (MOST 103-2221-E-033-039).
Publisher Copyright:
© 2015 Elsevier B.V.
PY - 2015/4/1
Y1 - 2015/4/1
N2 - The principle of immobilized metal affinity chromatography (IMAC) has been recently implemented for protein microarrays for the study of protein abundance and function. Ni-Co film fabricated by electrodeposition is a novel microarray surface in an alloy type for immobilizing histidine-tagged proteins based on IMAC. In this paper, the effects of crystallographic structures and surface properties of Ni-Co coatings, with and without the annealing process, on the immobilization of histidine-tagged proteins were systematically investigated. The experimental results reveal that the stronger hcp texture, due to a higher Co content, results in better affinity adsorption for histidine-tagged biotin. Nevertheless, the allotropic phase transformation from hcp to fcc, due to the annealing process, leads to the decrease of affinity adsorption. The wettability property and the surface roughness of Ni-Co coating are, however, not important factors. Obviously, the crystallographic structure of Ni-Co coating is the dominant factor for the specific affinity adsorption of histidine-tagged protein.
AB - The principle of immobilized metal affinity chromatography (IMAC) has been recently implemented for protein microarrays for the study of protein abundance and function. Ni-Co film fabricated by electrodeposition is a novel microarray surface in an alloy type for immobilizing histidine-tagged proteins based on IMAC. In this paper, the effects of crystallographic structures and surface properties of Ni-Co coatings, with and without the annealing process, on the immobilization of histidine-tagged proteins were systematically investigated. The experimental results reveal that the stronger hcp texture, due to a higher Co content, results in better affinity adsorption for histidine-tagged biotin. Nevertheless, the allotropic phase transformation from hcp to fcc, due to the annealing process, leads to the decrease of affinity adsorption. The wettability property and the surface roughness of Ni-Co coating are, however, not important factors. Obviously, the crystallographic structure of Ni-Co coating is the dominant factor for the specific affinity adsorption of histidine-tagged protein.
UR - http://www.scopus.com/inward/record.url?scp=84923364100&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84923364100&partnerID=8YFLogxK
U2 - 10.1016/j.colsurfb.2015.02.018
DO - 10.1016/j.colsurfb.2015.02.018
M3 - Article
C2 - 25731093
AN - SCOPUS:84923364100
SN - 0927-7765
VL - 128
SP - 55
EP - 60
JO - Colloids and Surfaces B: Biointerfaces
JF - Colloids and Surfaces B: Biointerfaces
ER -