|Vol. 18, No. 13||Dec. 3, 1998|
For the second consecutive year, a UD undergraduate claimed the top prize in the National Student Paper Competition during the American Institute of Chemical Engineers (AIChE) annual meeting in November.
Sujata Kumari Bhatia, 20, received the organization's coveted Edwin O. Eisen Award, which recognized her investigations of protein folding-a field with crucial implications for the medical, biotechnology and chemical manufacturing industries.
Bhatia, the daughter of Kanak and Kamlesh Bhatia of Newark, is simultaneously pursuing three different undergraduate degrees-in chemical engineering, biochemistry and biotechnology-as well as her master's degree in chemical engineering, under the direction of faculty member Anne Skaja Robinson. Her research with Robinson previously had won a regional AIChE competition, making her one of 10 finalists nationwide in the running for the first-place prize.
Last year, the same prize was awarded to Aaron Scurto, now a graduate student at Notre Dame University, whose undergraduate work at UD was supervised by Stanley I. Sandler, Henry Belin du Pont Professor of Chemical Engineering.
Bhatia's honor was one of nine national awards distributed during the 1998 AIChE meeting, reported Sandler, who served as the meeting's overall technical chairperson for 1998, with departmental colleague, Jon H. Olson, the vice chairperson.
Why study protein folding?
When proteins don't fold from a straight chain into a specific, three-dimensional shape, Bhatia explained, a variety of diseases may result. Alzheimer's disease, certain forms of cancer, cystic fibrosis and many other disorders are associated with improper folding by proteins, she said.
And, in the chemical industry, misfolding can increase product manufacturing and purifying costs.
So, Bhatia set out to learn how different chemical environments and starting materials would affect the folding of a model protein, "tailspike," within two host systems: the bacterium, Escherichia coli, and a mutant, more heavily oxidized cousin. She investigated mutant forms of the tailspike protein, too, Robinson said.
A component of the bacterial virus, P22, the tailspike protein had already been well-characterized by Robinson and, therefore, could be more easily investigated in the laboratory, Bhatia said.
To date, UD research has shown that "the more oxidizing environment" of the mutant E. coli strain seems to encourage correct folding by tailspike, she reported. Moreover, Robinson said, key building blocks of the protein- specifically, the amino acid, cysteine-play a critical role in proper folding. "Mutation of these cysteines leads to misfolding or aggregation that cannot be rescued by an oxidizing cellular (chemical) environment," Robinson said.
Someday, the UD research may help boost the yield of properly folded proteins during chemical manufacturing. It also may suggest possible strategies for preventing misfolding by other proteins tied to diseases. "If I can vary the environment in E. coli cells to encourage proper folding by this protein," Bhatia noted, "then maybe there's a way to correct folding errors common to other proteins, even within the human body."
Also during the AIChE meeting, Rakesh Agrawal of Air Products, who received his master's degree in chemical engineering from UD while working with Sandler in 1977, received the 1998 Institute Award for Excellence in Industrial Gas Technology.
The Award for Chemical Engineering Practice was conferred upon Vincent L. Magnotta of Air Products. Magnotta received his master's degree in chemical engineering from UD in 1966.
The AIChE meeting drew some 4,600 attendees who heard more than 3,000 technical presentations, Sandler said.