Direct evidence of ZnO morphology modification via the selective adsorption of ZnO-binding peptides
Liang, Mei-Keat and Deschaume, Olivier and Patwardhan, Siddharth V. and Perry, Carole C. (2011) Direct evidence of ZnO morphology modification via the selective adsorption of ZnO-binding peptides. Journal of Materials Chemistry, 21 (1). pp. 80-89. ISSN 0959-9428 (https://doi.org/10.1039/c0jm02124e)
Preview |
PDF.
Filename: c0jm02124e.pdf
Final Published Version Download (489kB)| Preview |
Abstract
Biomolecule-mediated ZnO synthesis has great potential for the tailoring of ZnO morphology for specific application in biosensors, window materials for display and solar cells, dye-sensitized solar cells (DSSCs), biomedical materials, and photocatalysts due to its specificity and multi-functionality. In this contribution, the effect of a ZnO-binding peptide (ZnO-BP, G-12: GLHVMHKVAPPR) and its GGGC-tagged derivative (GT-16: GLHVMHKVAPPRGGGC) on the growth of ZnO crystals expressing morphologies dependent on the relative growth rates of (0001) and (10 (1) over bar0) planes of ZnO have been studied. The amount of peptide adsorbed was determined by a depletion method using oriented ZnO films grown by Atomic Layer Deposition (ALD), while the adsorption behavior of G-12 and GT-16 was investigated using XPS and a computational approach. Direct evidence was obtained to show that (i) both the ZnO-BP identified by phage display and its GGGC derivative (GT-16) are able to bind to ZnO and modify crystal growth in a molecule and concentration dependent fashion, (ii) plane selectivity for interaction with the (0001) versus the (10 (1) over bar0) crystal planes is greater for GT-16 than G-12; and (iii) specific peptide residues interact with the crystal surface albeit in the presence of charge compensating anions. To our knowledge, this is the first study to provide unambiguous and direct quantitative experimental evidence of the modification of ZnO morphology via (selective and nonselective) adsorption-growth inhibition mechanisms mediated by a ZnO-BP identified from phage display libraries.
-
-
Item type: Article ID code: 31535 Dates: DateEvent2011Published22 October 2010Published OnlineSubjects: Technology > Chemical technology
Science > ChemistryDepartment: Faculty of Engineering > Chemical and Process Engineering
Technology and Innovation Centre > Bionanotechnology
Technology and Innovation Centre > Continuous Manufacturing and Crystallisation (CMAC)Depositing user: Pure Administrator Date deposited: 09 Jun 2011 15:36 Last modified: 28 Nov 2024 01:07 URI: https://strathprints.strath.ac.uk/id/eprint/31535