4.7 Article

Crystallographic structure of Ni-Co coating on the affinity adsorption of histidine-tagged protein

Journal

COLLOIDS AND SURFACES B-BIOINTERFACES
Volume 128, Issue -, Pages 55-60

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.colsurfb.2015.02.018

Keywords

Immobilized metal affinity chromatography (IMAC); Affinity adsorption; Histidine; Electrodeposition; Crystallographic structure

Funding

  1. Ministry of Science and Technology (MOST) of Taiwan, R.O.C. [MOST 103-2221-E-033-039]

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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 electrode-position 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. (c) 2015 Elsevier B.V. All rights reserved.

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