Title:
The protein and peptide mediated syntheses of non-biologically-produced oxide materials

dc.contributor.advisor Sandhage, Kenneth H.
dc.contributor.advisor Kröger, Nils
dc.contributor.advisor Naik, Rajesh
dc.contributor.author Dickerson, Matthew B. en_US
dc.contributor.committeeMember Hud, Nicholas
dc.contributor.committeeMember Marder, Seth
dc.contributor.department Materials Science and Engineering en_US
dc.date.accessioned 2008-09-17T19:30:55Z
dc.date.available 2008-09-17T19:30:55Z
dc.date.issued 2007-07-09 en_US
dc.description.abstract The research detailed in this dissertation is focused on the use of biomolecules (i.e., peptides and proteins) to form non-biologically produced materials under mild reaction conditions (i.e, neutral pH, aqueous solutions, and room temperature). The peptides utilized in the studies detailed in this dissertation were identified through the screening of single crystal rutile TiO2 substrates or Ge powder with a phage-displayed peptide library. Twenty-one peptides were identified which possessed an affinity for Ge. Those peptides possessing a basic isoelectric point as well as hydroxyl- and imidazole-containing amino acid residues were found to be the most effective in precipitating amorphous germania from an alkoxide precursor. The phage-displayed peptide library screening of TiO2 substrates yielded twenty peptides. The titania formation activity of these peptides was found to correlate with the number of positive charges they carried. The titania materials generated by the library-identified and designed peptides were found to be composed of amorphous titania as well as <10 nm anatase and/or monoclinic TiO2 crystallites. Four recombinant proteins, derived from the amino acid sequences of proteins (silaffins) associated with biosilicification in diatoms, were also investigated for titania precipitation activity. The two most basic of these recombinant silaffins, rSil1L and rSilC, were able to induce the formation of titania. The titania precipitates generated by rSil1L were found to be similar to those produced by the phage-displayed library identified peptides. The second recombinant silaffin, rSilC, was found to produce hollow spheres of titania, which, following dehydration, were observed to transform into larger, solid spheres composed of radially aligned columns of rutile TiO2. The highly repetitive nature of the rSilC s amino acid sequence is believed to be responsible for the differences in TiO2 polymorph generated by the different recombinant silaffins and peptides. This dissertation also details research conducted on the formation of titania utilizing rSilC conjugated to synthetic and biogenic silica surfaces. These silica surfaces were functionalized with a newly developed drendritic growth technique. The dendritic functional-group amplification process was demonstrated to increase the loading of hexahisitidine tagged proteins on silica surfaces by more than 40%, as compared to traditional immobilization procedures. en_US
dc.description.degree Ph.D. en_US
dc.identifier.uri http://hdl.handle.net/1853/24704
dc.publisher Georgia Institute of Technology en_US
dc.subject Phage display en_US
dc.subject Biomimetic en_US
dc.subject Germania en_US
dc.subject Titania en_US
dc.subject.lcsh Oxides Synthesis
dc.subject.lcsh Biomolecules
dc.subject.lcsh Diatoms Frustules
dc.subject.lcsh Self-assembly (Chemistry)
dc.subject.lcsh Diatoms Genetic engineering
dc.title The protein and peptide mediated syntheses of non-biologically-produced oxide materials en_US
dc.type Text
dc.type.genre Dissertation
dspace.entity.type Publication
local.contributor.corporatename School of Materials Science and Engineering
local.contributor.corporatename College of Engineering
relation.isOrgUnitOfPublication 21b5a45b-0b8a-4b69-a36b-6556f8426a35
relation.isOrgUnitOfPublication 7c022d60-21d5-497c-b552-95e489a06569
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