Monday, November 12, 2012
Grad student Yuqin Shang publishes paper in the journal Analytical ChemistryGraduate student Yuqin Shang, of the Department of Chemistry, is the lead author on a publication in the October 2nd issue of the journal Analytical Chemistry (Volume 84, Pages 8164-8170). The paper, titled Characterization of the Native and Denatured Herceptin by Enzyme Linked Immunosorbent Assay and Quartz Crystal Microbalance Using a High-Affinity Single Chain Fragment Variable Recombinant Antibody, was coauthored by Shang’s mentor, CBR member Xiangqun Zeng. Shang is enrolled in the Biomedical Sciences: Health and Environmental Chemistry PhD program. One of Shang’s earlier papers was mentioned in the CBR News previously. Parts of the introduction to the recent paper are reproduced below.
"Chimeric, humanized, and fully human therapeutic antibodies
and antibody fragments are gaining widespread use
for the treatment of various human diseases such as arthritis,
autoimmune diseases, allergy, cardiovascular disease, transplantrejection, cancer, and viral infections. These therapeutic
protein drugs can be extraordinarily expensive, with some
treatments costing $100,000 or more per year. Therapeutic
proteins that aggregate or denature upon storage may lose
biological activity and cannot be used in humans…. It can be costly and time-consuming to determine if
therapeutic antibodies in solution have aggregated or denatured
when produced or stored. We used phage display and quartzcrystal microbalance (QCM) to develop a rapid, highly
sensitive single chain fragment variable (scFv)-based piezoimmunosensor
assay to detect aggregated and degraded Herceptin
in solution. This and similar assays can potentially be used to
monitor therapeutic antibodies to quickly identify optimal
conditions under which antibodies can be produced, formulated,
stored, and used to retain biological activity."
Zeng will discuss related work at the Oakland University Beaumont Biomedical Research Symposium in the Oakland Center Banquet Hall on November 14.
This research is supported by the National Institutes of Health (R21EB006495)