Developing Biotemplated Data Storage: Room Temperature Biomineralization of L10 CoPt Magnetic Nanoparticles

Johanna Galloway, Jennifer Talbot, Kevin Critchley, Jim Miles, Jonathan Bramble

Research output: Contribution to journalArticle (Academic Journal)peer-review

29 Citations (Scopus)
602 Downloads (Pure)

Abstract

L10 cobalt platinum can be used to record data at approximately sixfold higher densities than it is possible to on existing hard disks. Currently, fabricating L10 CoPt requires high temperatures (≈500 °C) and expensive equipment. One ecological alternative is to exploit biomolecules that template nanomaterials at ambient temperatures. Here, it is demonstrated that a dual affinity peptide (DAP) can be used to biotemplate L10 CoPt onto a surface at room temperature from an aqueous solution. One part of the peptide nucleates and controls the growth of CoPt nanoparticles from solution, and the other part binds to SiO2. A native silicon oxide surface is functionalized with a high loading of the DAP using microcontact printing. The DAP biotemplates a monolayer of uniformly sized and shaped nanoparticles when immobilized on the silicon surface. X-ray diffraction shows that the biotemplated nanoparticles have the L10 CoPt crystal structure, and magnetic measurements reveal stable, multiparticle zones of interaction, similar to those seen in perpendicular recording media. This is the first time that the L10 phase of CoPt has been formed without high temperature/vacuum treatment (e.g., annealing or sputtering) and offers a significant advancement toward developing environmentally friendly, biotemplated materials for use in data storage.
Original languageEnglish
Pages (from-to)4590-4600
Number of pages11
JournalAdvanced Functional Materials
Volume25
Issue number29
Early online date15 Jun 2015
DOIs
Publication statusPublished - 5 Aug 2015

Research Groups and Themes

  • Bristol BioDesign Institute

Keywords

  • Biomineralization
  • MAGNETIC NANOPARTICLES
  • biotemplate
  • data storgae
  • dual affinity peptides
  • SYNTHETIC BIOLOGY

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