Effect of proteins on the self-assembly of multiring structural ZrO2nanodisks

  • Ji H
  • Liu X
  • Wang X
 et al. 
  • 4

    Readers

    Mendeley users who have this article in their library.
  • 11

    Citations

    Citations of this article.

Abstract

Compared to the air-water interfacial zirconia film with regularly multiring structure self-assembled by using zirconium(IV) butoxide as precursor, sodium dodecyl sulfonate (SDS) as template and gelatin (G) as stabilizer, another kind of multiring structural ZrO2nanodisks has been prepared in the presence of the globular protein bovine serum albumin (BSA). X-ray diffraction (XRD), scanning electron microscope (SEM), transmission electron microscope (TEM) and X-ray photoelectron spectroscopy (XPS), etc. have been used to characterize morphologies, high ordered structures and components for the assembled ZrO2film. Results show that both G and BSA could help to assemble multiring structural ZrO2films. The difference is that the multiring nanodisk assembled with BSA seems to be relatively defective compared to the product prepared with G, due to the better ability of G to stabilize the micelles of surfactant templates. Remarkably, this self-assembly method may be widely applied in preparing many functional metal oxide nanofilms and proteins will play important roles in assembling well ordered structures inside those films. © 2009.

Author-supplied keywords

  • Air-water interface
  • BSA
  • Multiring
  • Self-assemble
  • ZrO2film

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free