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magazine home > archives > fall 2001 > features

While Abby Parrill says most people understand the motivation and anticipated results of her research, many cannot comprehend the method. But she has it down to a science. "Simplify it," says the assistant professor of chemistry.

Keeping it Simple
by Kristen Epler

Dr. Abby Parrill with research team
Dr. Abby Parrill (center) and her team of researchers, including graduate students Charlie Singer (left) and Hongbin Yuan (right), use computers to simplify and study the chemical receptors of molecules, like the one pictured here.

The human body is made up of a complicated system of amino acid chains, molecules and chemical receptors, among other things. Making sense of it can often lead to frustration and bewilderment. But a U of M assistant professor of chemistry has discovered the perfect way to analyze these biological systems, and she is using it to make significant strides in research that could help save others from deadly diseases.

Since arriving at the University in 1996, Dr. Abby Parrill has been "simplifying" the study of molecules and chemical receptors to find ways these particles can be synthetically modified to produce better prescription drugs. Specifically, she and her research team use computers to study biologicalmolecules, and how these molecules, or growth factors, interact with proteins in the body.

"The growth factors that we are studying affect wound healing, cell migration and vascular, or blood vessel, development," Parrill says. "Synthetic molecules could be designed to mimic the natural ones. These natural molecules don't make good drugs, but the synthetic molecules could. The modification of these molecules could lead to improvements in the treatments of certain types of cancer and tumors. It could also aid neonatal development, the healing time of burn victims and increase the viability of organ transplants."

Parrill's work begins with reports from other research groups on "interesting" proteins. Proteins, made up of amino acid chains, are classified into specific types. One kind of protein is a set of receptors embedded in the membrane surrounding a human cell. These receptors that intercept chemical signals from outside the cell and inform the cell about the signal are the focus of Parrill's research.

"Receptors are useful biological systems that we might want to influence," Parrill says. "Sixty percent of known drugs interact with the receptors we are studying in order to take effect."

To analyze these interactions, Parrill's team builds computer-generated models of the receptors and simplifies them even further to the individual amino acids that make up each receptor's structure. Biologists and molecular biologists then test the hypotheses generated from these models in test tubes.

The results provide useful information to synthetic chemists regarding chemical modifications that can be made to the signal molecules in order to produce the desired response from the receptor.

The path from pure research to clinically useful drugs takes many years and many additional researchers. If desired results are achieved by Parrill's team, and subsequent animal testing indicates the modified molecules are safe, clinical testing then begins on small groups of healthy humans. Once proven safe in humans, the effect must be demonstrated on a sample of people with a health problem targeted by the studied disease. Final tests are then conducted on larger populations. If all procedures prove favorable, the molecules can be produced for medicinal use.

"The whole process from start to finish takes 10 years or more before it reaches the clinic where it can be used for therapeutic treatments," Parrill says.

Parrill's crew has already made a significant stride toward its overall goal of understanding how the receptors recognize the signaling molecules. "The protein has 400 amino acids," she says. "We identified one position out of the 400 that, when changed, could make a receptor recognize a different molecule, or growth factor."

The finding was verified and put the group one step closer to identifying what can be done to synthetically duplicate the effect of the natural growth factors.

Parrill is not the only one who believes in the power of this work. The American Heart Association has committed $70,000 to her research in collaboration with the University of Tennessee Health Science Center-Memphis every year between 1999 and 2001. The National Science Foundation has granted her $150,000 in support of summer research programs. The National Institutes of Health is also funding Parrill's research with a three-year, $75,000 grant.

Yet, for this researcher bestowed with many accolades, including an Early Career Research Award from the College of Arts and Sciences, the rewards of her work extend beyond personal honors and pharmaceutical benefits.

"I really get a lot of enjoyment out of seeing my students learn to do and enjoy research," Parrill says.
Her current team of 10 student researchers seems to be doing just that. In the Smith Hall labs on campus that make up the Computational Research on Materials Institute (CROMIUM), they continue simplifying biological complexities, receiving occasional help from UT, the University of Alberta, Georgetown, Ohio State and other U of M faculty.

"It's fascinating to understand how the simple principles of chemistry work in very complex systems," Parrill says. "When you focus tightly on small parts of large protein structures, they're as easy to understand as basic chemistry."

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