"My experience as a research student is priceless. I wouldn't trade it for anything.”
Armstrong research could lead to pharmaceutical breakthrough
A research team at Armstrong Atlantic State University is conducting groundbreaking biocatalysis research with the potential to transform the way enzymes are used to synthesize heart medication, antidepressants and other popular prescription drugs.
Biocatalysis, a process that performs chemical transformations, has been around for centuries and played a key role in the manufacturing of beer, wine, cheese and bread. Recent technological advances in DNA have made available to scientists the sequences of several microorganism genomes, spurring the growth of new and important contributions of biocatalysis to the pharmaceutical industry.
Armstrong faculty and students are now adding to those contributions. The university's interdisciplinary research team, composed of assistant professor of biology Scott Mateer and assistant professors of chemistry Brent Feske and Cliff Padgett, received grant funding from the National Science Foundation to conduct the research.
“We've carved out a niche here at Armstrong,” says Dr. Mateer. “We want to understand how enzymes work so we can improve our ability to predict which enzymes work best on specific molecules to give us our desired chemistry. In essence, we're using chemistry to find efficient ways to create the drugs people use every day.”
Faye Montgomery, a senior pursuing a B.S. in biology, enjoys the opportunity to contribute to the ongoing research. She is currently helping to study enzymes in baker's yeast, analyzing the potential for resulting compounds to be used in pharmaceutical production.
“The most exciting part of the research is when I see the data come together to paint a picture of our enzyme's structure and function,” she says. “I have learned so much about biochemistry and molecular biology. My experience as a research student is priceless. I wouldn't trade it for anything.”
The group is specifically interested in studying a family of yeast enzymes called reductases, which are significant because they can produce chiral alcohols. These particular alcohols are important building blocks for several medications. Working closely with undergraduate students, the research group uses the enzymes to produce either “right-handed” or “left-handed” alcohols. “That's critical, because in medicine the stereospecificity, or handedness of the molecule, is extremely important,” Dr. Mateer explains. “The right-handed molecule can be the active ingredient in the medicine, but the left-handed molecule can be inert or even cause birth defects.”
Using a library of enzymes, the biocatalysis research team combines various molecules with enzymes and then determines the stereospecificity of the resulting product. The team also mutates these enzymes in strategic ways to understand how they accomplish the desired chemistry. Obtaining this knowledge can lead to major pharmaceutical breakthroughs.
“This whole process is being driven by the pharmaceutical industry as they strive to find cost-efficient methods to synthesize popular drugs,” says Dr. Mateer. “Biocatalysis can be easier and more environmentally friendly than other manufacturing processes, resulting in methods that are potentially faster and cheaper than ever before.”