Rebecca J. Whelan,
Assistant Professor, at Oberlin since 2005

Research Interests:
bioanalytical chemistry, aptamers, biosensors, capillary electrophoresis 

Research in the Whelan lab is in the area of bioanalytical chemistry. Our work centers on the use of biological affinity interactions, microscale separations, and surface-sensitive spectroscopy to detect biomarkers of ovarian cancer. Related work involves the development of nucleic acid aptamers for targets of clinical importance. Other collaborative work in chemical ecology is developing. Four major projects are currently ongoing:

Project 1: Selection of an aptamer that recognizes CA125
The selective detection of biomolecules in serum is an important tool for basic research and clinical applications. Traditionally, such assays have relied on antibody molecules as the basis of detection. In this project we explore a relatively new class of affinity molecules--aptamers--and develop analytical assays that exploit their unique advantages. We are working on the selection a DNA aptamer that recognizes CA125, a protein that is widely used as an ovarian cancer biomarker.

Project 2: Development of an antibody-based SPR assay for the ovarian cancer biomarker CA125
In this project, we seek to develop an immunoassay to detect the ovarian cancer marker CA125 using surface plasmon resonance spectroscopy (SPR). SPR is a label-free method for detecting proteins and characterizing biomolecular interactions. Selective deposition of antibody molecules that recognize CA125 will enable the creation of a selective, sensitive, and label-free assay for this important cancer biomarker.

Project 3: Synthesis and characterization of a peptide biomarker mimic
A long-term goal of the Whelan lab is the development of a nucleic acid ligand (aptamer) that recognizes the ovarian cancer biomarker CA125. The gene that codes for CA125 was recently discovered, revealing CA125 to be a very large (2 million dalton) protein with variable numbers of repeated domains and abundant, variable glycosylation. To simplify the process of aptamer selection, we have synthesized a small peptide that contains the antibody recognition site, thus serving as a mimic for the much larger intact protein. Characterization and application of this peptide is ongoing.

Project 4: Characterization of the volatile compounds of the uropygial secretions of the grey catbird
This project is a collaboration with Professor Mary Garvin of the Oberlin Biology Department. The uropygial gland of birds, also known as the preen gland or oil gland, produces secretions that are important in maintaining the health and structural integrity of feathers. These secretions are believed to have a number of functions including waterproofing and conditioning the feathers, as well as protection from insect pests and predators. This project involves the use of solid-phase microextraction to sample the volatiles in uropygial secretions from catbirds, followed by gas chromatography-mass spectrometry for compound identification.

BA, Lawrence
PhD, Stanford