Polarization behavior of bulk Zr-base amorphous alloy immersed in cell culture medium

Sachiko Hiromoto, An Pang Tsai, Masae Sumita, Takao Hanawa

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

Effects of amino acids and proteins on polarization behavior of Zr-base amorphous alloy were examined using Hanks' solution, minimum essential medium (MEM), and cell culture medium (MEM+FBS) consisting with MEM and fetal bovine serum (FBS), respectively. Amorphous powder consolidated Zr55Al10Ni10Cu15 alloy was cathodically and anodically polarized at the beginning of (after 1.8 ks) immersion and after a long-term (605 ks) immersion in each solution. Parameters on the anodic polarization curve; open-circuit potential (Eopen), polarization resistance (Rp), and pitting potential (Epit), were obtained for the examination of corrosion resistance. In the presence of amino acids and proteins, Rp and Epit increased, indicating that resistance to both general and pitting corrosion was raised with those biomolecules. Thus, the adsorbed biomolecules probably work as a diffusion barrier to molecules and ions such as dissolved oxygen and phosphate and chloride ions. During immersion, the surface oxide film grew, leading to the increase in Eopen, average Epit, and Rp although the parameters showed wide variance of deviation probably caused by the defects in alloy structure. The lowest values of Epit after the long-time immersion were not lower than those at the beginning of immersion, indicating that the sensitivity of defects to chloride ion was not enhanced during immersion. However, the pitting corrosion resistance decreased during immersion because the potential difference between Eopen and Epit decreased.

Original languageEnglish
Pages (from-to)3112-3117
Number of pages6
JournalMaterials Transactions
Volume43
Issue number12
DOIs
Publication statusPublished - 2002 Dec

Keywords

  • Amino acids
  • Amorphous powder consolidated zirconium-base alloy
  • Biomaterial
  • Cell culture medium
  • Immersion term
  • Polarization
  • Proteins

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