Degree Type

Dissertation

Date of Award

2003

Degree Name

Doctor of Philosophy

Department

Chemistry

First Advisor

Marc D. Porter

Abstract

The future advancement of nearly all basic and applied sciences is linked in some aspect to understanding and/or controlling of events that occur on the nanometer size scale. One such tool that is being investigated to assist in these studies is nanoparticles. This thesis revolves around the theme of self-assembling nanoparticles to either understand the behavior of the nanoparticles themselves or create analytically useful architectures. The beginning of this thesis examines the interplay between various polymeric nanoparticle properties (i.e., surface chemistry) and patterns of monolayers that display differing chemical moieties. This investigation then leads to the development of guidelines for building two-dimensional patterns through solution deposition and self-assembly of nanoparticles on the underlying.;The properties of polymeric nanoparticles are further employed to create miniaturized platforms with a process involving both the layer-by-layer and photolithographic methodologies. This scheme creates structures with control over the magnitude of all three-dimensions. The analytical utility of the three dimensional structures is demonstrated through creation of a massively dense array of sub-femtoliter volume wells. These microwells are shown to be capable of isolating compounds micrometers apart from one another. Moreover, this characteristic, along with other properties of these wells, is exploited to develop a miniaturized, immunodiagnostic platform.;Finally, the theme of self-assembly of nanoparticles for the purpose of immunodiagnostics is advanced through the creation of a unique height based, "bar-code" read-out concept. The surfaces of gold and silica nanoparticles are designed to aggregate in a pre-determined pattern when in the presence of a specific analyte. An atomic force microscope (AFM) is employed to analyze the "bar-code" design and positively identify the presence of the analyte. A proof-of-concept experiment with that exploits the specificity of biotin-streptavidin binding is employed to validate the concept.

DOI

https://doi.org/10.31274/rtd-180813-9888

Publisher

Digital Repository @ Iowa State University, http://lib.dr.iastate.edu

Copyright Owner

Andrew David Pris

Language

en

Proquest ID

AAI3118253

File Format

application/pdf

File Size

212 pages

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