Effect of proteins on the self-assembly of multiring structural ZrO2 nanodisks

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 ZrO2 nanodisks 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 ZrO2 film. Results show that both G and BSA could help to assemble multiring structural ZrO2 films. 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.