Date of Award

5-2007

Degree Name

Doctor of Philosophy

Department

Chemistry

First Advisor

Dr. Subra Muralidharan

Second Advisor

Dr. Brian C. Tripp

Third Advisor

Dr. Nora Berrah

Fourth Advisor

Dr. Yirong Mo

Abstract

Flagella of Mesophilic bacteria such as E. coli are extremely ordered structures consisting of self-assemblies of flagellin 11-mers resulting in protein nanotubes of 2--3 nm inner diameter, 23 nm outer diameter, several microns in length and 5.4 nm separation between 11-mer segments. They are as a result attractive scaffolds and templates for the generation of uniform nanotubes and ordered array of nanoparticles. In this study fusion protein of bacterial flagellin (Fli C) and core thioredoxin (Trx), pFliTrx was used as peptide display on bacterial flagella. This was accomplished in the current research by introducing various peptide loops such as cysteine, histidine, arginine-lysine, tyrosine-serine-lysine, and aspartic acid-glutamic acid in the multiple cloning site of the thioredoxin core of the FliTrx fusion protein by site directed mutagenesis and cassette mutagenesis. The flagella formed from these flagellin proteins expressed in E. coli bacteria were harvested, purified, and characterized. Various metal ions such as Cu(II), Cd(II), Ag(I), Au(I), Au(III) were bound to histidine and aspartic acid-glutamic acid peptide loops and reduced in a controlled manner to generate nanoparticle arrays and nanotubes. Silicate and titanate ions were bound to arginine-lysine and tyrosine-serine-glycine peptide loops respectively and polymerized to obtained silica and titania nanotubes. Polyaniline nanotubes and hydroxyapatite nanoparticles were also generated on aspartic acid-glutamic acid peptide loops.

Comments

5th Advisor: Dr. Dongil Lee

Access Setting

Dissertation-Open Access

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