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The protein and peptide mediated syn...

Georgia Institute of Technology.

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

Record Type:	Language materials, printed : Monograph/item
Title/Author:	The protein and peptide mediated syntheses of non-biologically-produced oxide materials./
Author:	Dickerson, Matthew B.
Description:	145 p.
Notes:	Advisers: Kenneth H. Sandhage; Nils Kroger; Rejesh R. Naik.
Contained By:	Dissertation Abstracts International69-09B.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3327559
ISBN:	9780549805793

The protein and peptide mediated syntheses of non-biologically-produced oxide materials.
Dickerson, Matthew B.

The protein and peptide mediated syntheses of non-biologically-produced oxide materials. - 145 p.

Advisers: Kenneth H. Sandhage; Nils Kroger; Rejesh R. Naik.

Thesis (Ph.D.)--Georgia Institute of Technology, 2008.

Numerous examples exist in nature of organisms which have evolved the ability to produce sophisticated structures composed of inorganic minerals. Studies of such biomineralizing organisms have suggested that specialized biomolecules are, in part, responsible for the controlled formation of these structures. 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).

ISBN: 9780549805793Subjects--Topical Terms:

1017719
Biology, Molecular.

The protein and peptide mediated syntheses of non-biologically-produced oxide materials.
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020 $a 9780549805793
035 $a (UMI)AAI3327559
035 $a AAI3327559
040 $a UMI $c UMI
100 1 $a Dickerson, Matthew B. $3 1029272
245 1 4 $a The protein and peptide mediated syntheses of non-biologically-produced oxide materials.
300 $a 145 p.
500 $a Advisers: Kenneth H. Sandhage; Nils Kroger; Rejesh R. Naik.
500 $a Source: Dissertation Abstracts International, Volume: 69-09, Section: B, page: 5700.
502 $a Thesis (Ph.D.)--Georgia Institute of Technology, 2008.
520 $a Numerous examples exist in nature of organisms which have evolved the ability to produce sophisticated structures composed of inorganic minerals. Studies of such biomineralizing organisms have suggested that specialized biomolecules are, in part, responsible for the controlled formation of these structures. 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).
520 $a 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 phagedisplayed peptide library. Twenty-one peptides were identified which possessed an affinity for Ge. Three of these twenty one peptides were tested for germania precipitation activity. 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.
520 $a The phage-displayed peptide library screening of TiO2 substrates yielded twenty peptides. Four of these peptides, which were heavily enriched in histidine and/or basic amino acid residues, were found to possess signficant titania precipitation activity. The activity of these peptides was found to correlate with the number of positive charges they carried. The sequence of the most active of the library-identified peptides was modified to yield two additional peptides. The titania precipitation activity of these designed peptides was higher than the parent peptide, with reduced pH dependence. 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.
520 $a The production of titania and zirconia resulting from the interaction of the cationic enzyme, hen egg white lysozyme, with Ti- or Zr-lactate precursors is also presented in this dissertation. Lysozyme was found to entrap itself in an active form within the nanoparticles of amorphous titania or zirconia precipitated by this protein under ambient conditions. The lysozyme synthesized titania was observed to be superior to the lysozyme-zirconia materials in preserving the activity of the enzyme under denaturing conditions.
520 $a 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.
520 $a 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. The higher loadings of rSilC provided by this dendritic growth method were observed to have a positive impact on the extent of surface mineralization. The titania formed by immobilized rSilC was observed to be composed of amorphous and crystalline TiO2.
590 $a School code: 0078.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Chemistry, Inorganic. $3 517253
650 4 $a Engineering, Materials Science. $3 1017759
690 $a 0307
690 $a 0488
690 $a 0794
710 2 $a Georgia Institute of Technology. $3 696730
773 0 $t Dissertation Abstracts International $g 69-09B.
790 $a 0078
790 1 0 $a Kroger, Nils, $e advisor
790 1 0 $a Naik, Rejesh R., $e advisor
790 1 0 $a Sandhage, Kenneth H., $e advisor
791 $a Ph.D.
792 $a 2008
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3327559