Date of Award

Spring 5-2013

Degree Type

Dissertation

Degree Name

Doctor of Philosophy (PhD)

Department

Polymers and High Performance Materials

Committee Chair

Sarah Morgan

Committee Chair Department

Polymers and High Performance Materials

Committee Member 2

Robert Lochhead

Committee Member 2 Department

Polymers and High Performance Materials

Committee Member 3

Charles McCormick

Committee Member 3 Department

Polymers and High Performance Materials

Committee Member 4

Sabine Heinhorst

Committee Member 4 Department

Chemistry and Biochemistry

Committee Member 5

Gordon Cannon

Committee Member 5 Department

Chemistry and Biochemistry

Committee Member 6

Sergei Nazarenko

Committee Member 6 Department

Polymers and High Performance Materials

Abstract

Naturally occurring macromolecules are produced for a specific function and have the selectivity to accomplish objectives with little waste in energy. The scientific community strives to develop smart, efficient molecules on an economical scale, thus lessons can be learned from nature and applied to cost effective synthetic systems. First, the mimicry of naturally occurring antimicrobial peptides (AMPs) will be described. AMPs show great potential as alternatives to conventional antibiotics as they can selectively bind and eliminate pathogenic bacteria without harming eukaryotic tissues. Aqueous reversible addition–fragmentation chain transfer (RAFT) polymerization was utilized to prepare primary and tertiary amine containing AMP polymer mimics with precise polymerization control. The detailed synthetic strategy along with an outline of in vitro cell studies will be discussed in order to elucidate the effect of polymer composition on antimicrobial activity and selectivity.

The second section of this work will discuss a highly surface active protein from filamentous fungi called hydrophobin. Hydrophobins are small proteins that spontaneously self-assemble into polymeric films at interfaces. They are amphipathic in nature and form tightly bound membranes that shift the polarity of interfaces at which they assemble. This research focuses on elucidating the mechanisms and driving forces for assembly of the ABH1 hydrophobin protein from the edible white button mushroom Agaricus bisporus.

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