Date of Award

5-2009

Document Type

Thesis

Degree Name

Master of Science (MS)

Legacy Department

Chemistry

Advisor

Creager, Stephen E

Committee Member

Guiseppi-Elie , Anthony

Committee Member

Chumanov , George

Abstract

Proteins and nucleic acids play major roles in many important biological processes. Specific and rapid detection of these biomolecules is important for early and precise diagnosis of various genetic diseases and other medical conditions. However, accurate and inexpensive detection of proteins and nucleic acids has always been a challenge. One of the obstacles is their non-specific adsorption on the sensor surface which leads to the conformational changes in the proteins, sometimes causing their denaturation. The non-specific adsorption on the surface also leads to sensor fouling which induces changes in the availability of active sensor surface for detection of analytes and thus decreases the sensor response. Non-specific binding of biomolecules is therefore a major drawback of biosensor applications and its elimination or suppression needs to be carefully considered while developing biosensors.
The present work discusses various strategies to modify the surface of reticulated vitreous carbon (RVC) electrodes to suppress the non-specific binding of biomolecules. Both non-specific (NSB) and specific binding (SB) of neutravidin, oligonucleotides and enzyme labels were studied inside the pores of RVC electrodes that had been subjected to various modification schemes. The extent of NSB and SB of these biomolecules onto unmodified as well as modified RVC electrodes was compared by determining the initial rate of generation of an enzymatic product using linear scan voltammetry (LSV). A simple sandwich bioassay for detection of neutravidin (a deglycosylated version of avidin) was performed on the RVC electrode with the lowest NSB. The surface coverage of these biomolecules inside the RVC pores was estimated by spectroscopic as well as by electrochemical method.

Included in

Chemistry Commons

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