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

Yaw Jen Chang, Sheng Zheng Chen, Ching Yuan Ho

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)55-60
Number of pages6
JournalColloids and Surfaces B: Biointerfaces
Volume128
DOIs
Publication statusPublished - 2015 Apr 1

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Surfaces and Interfaces
  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

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