Developing a technique to assist in the design of new drugs without years of trial and error testing started with meticulous work at the molecular level in Jeffrey Boles' chemistry lab.

For his most recent contributions to his field, Boles, associate professor of Chemistry and director of our Environmental Sciences doctoral program, has been named this year's Sigma Xi Research Award winner. His paper, "Synthesis and Incorporation of [6,7]-selenatryptophan into dihydrofolate reductase," published in the 2002 issue of the internationally recognized journal Biochemical and Biophysical Research Communications, offers researchers around the world previously unavailable routes to explore the structure of proteins.

"It would be difficult to overemphasize the scientific importance of this work," says Chemistry Chairperson Scott Northrup.

In order to study drugs and their effects on the body, scientists must be able to study the architecture of proteins. Boles' work is at the forefront of his field because he has developed a new way to discover the structure of proteins.

"Think about how you've seen dozens of drug ads on television and in popular magazines that you didn't see years ago," says Boles. "A couple of decades ago, trial and error was the only way to effectively test if a drug served its intended purpose since the structure of the protein targets was unknown in most instances. Now that process is faster because of the kind of work we do, and drugs make it to market much faster.

"Without techniques of seeing what's happening with proteins, it's difficult to design drugs, study diseases, or even learn about the well-being of the body unless you can see what's happening on the molecular level," he explains.

In the late 1980s and early '90s, Boles developed a way to incorporate selenium and tellurium containing amino acids into proteins. This gave researchers an additional means of determining the 3-D architecture of proteins. This is now the method used most often by researchers worldwide.

"This recent publication adds one more tool to the arsenal researchers have to discover the molecular structure of proteins," says Boles.

Without the techniques pioneered by Boles, there still would be a lot of guesswork in how different drugs work. The use of this new unusual amino acid acts like a molecular-level camera and allows researchers to see how drugs inhibit and activate proteins in the body.

Although much of the work in this field is directed by Boles at Tennessee Tech, he gives credit to the circle of chemists, biochemists and physicists who work all across the country on this effort directed from his laboratory.

"Science today is cross-disciplinary," he says. "To succeed, you must embrace that." Boles' research dollars are generated from the National Science Foundation, Oak Ridge National Laboratory, Los Alamos National Laboratory and Tennessee Tech.

Sigma Xi is an international scientific research society. Each year, the Tennessee Tech chapter recognizes excellent scientific research by one faculty member for a research paper published or accepted for publication.

Boles was honored during our chapter's annual banquet. Other awards included honoring retired Chemical Engineering Professor David Yarbrough for his 20 years of service as secretary/treasurer.