I teach the following classes in analytical chemistry CHE 331, CHE 531, CHE 632, and CHE 570A.
 

Education:
1995     B.S. in Chemistry                                                                           Furman University
 2001   Ph.D in Analytical Chemistry with Professor Marc D. Porter          Iowa State University

Work Experience:  Camille and Henry Dreyfus Postdoctoral Fellow with Joe Pesek at San Jose State University.
 

Research Interests:

Research in my group is situated at the interface of analytical chemistry and biochemistry.  Specifically, we are developing new separations techniques for determining concentrations and actions of pharmaceuticals, peptides, and proteins.  We design novel stationary phases for high performance liquid chromatography (hplc) for the resolution of complex sample mixtures, and improve the reproducibility of capillary electrophoresis in the analysis biological molecules.  We further the use of capillary electrochromatography for the analysis of biological molecules.

Project I:    Development of affinity capillaries for the preconcetration of signaling peptides.

To transmit a signal from the cell membrane to the nucleus, most eukaryotic cells use phosphorylation/ dephosphorylation pathways in which kinases add phosphate groups to small peptides and phosphatases remove phosphate groups.  The phosphorylated and dephosphorylated peptides can be easily resolved by capillary electrophoresis, but identification of the peptides is difficult due to adsorption on the capillary wall.  Additionally, cellular concentrations of signal peptides are often below the detection limits of most instruments. We are using silanization and hydrosilation techniques to create capillaries modified with antibodies for the preconcentration of these signal peptides, and a coating that resists adsorption for the separation of the proteins. Additionally, we use laser induced fluorescence as a highly sensitive detection method for this system.

Project II: Development of Affinity Capillary Electrophoresis for the Determination of Pharmaceutical Binding Constants with their Membrane-bound Targets

Most pharmaceuticals target one of the three classes of membrane-bound receptor proteins during their mode of action.  The binding of the pharmaceutical to the protein is described by the binding constant which can be derived from concentration measurements of the free and bound forms of the drug.  For the measurement to be meaningful, the receptor must have the correct secondary and tertiary structure which dictates that it exist in a hydrophobic environment (liposome).  We are developing a technique to measure the binding constant of pharmaceuticals with liposome- encapsulated receptor molecules. The concentrations of the pharmaceuticals must be measured at very low concentrations, which dictates the use of laser induced fluorescence.

Project III: Development of Liquid-Crystal Stationary Phases for the Resolution of Pharmaceuticals

A liquid crystal demonstrates long range order that is not present in ordinary liquids, and this order can be manipulated with temperature.  When placed on a silica support, liquid crystal stationary phase molecules, interact with one another to form structures which influence the separation efficiency and resolution.  If the appropriate liquid crystal stationary phases can be developed, the retention properties could be manipulated through temperature instead of mobile phase composition.  We are working to develop such phases.