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COOKEVILLE, Tenn. (May 8, 2003) -- 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 at Tennessee Tech University.
For his most recent contributions to his field, Boles, an associate
professor of chemistry and director of TTU's environmental science doctoral
program, has been named TTU's 2003 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," said Scott Northrup, TTU chemistry department chairperson.
The significance of Boles' research is that in order to study drugs
and their effects on the body, scientists must be able to study the architecture
of proteins. His 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 seen dozens of drug ads on television and in popular
magazines that you didn't see years ago," said 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 were 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," explained
Boles.
In the late '80s 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 most often utilized method by researchers world
wide
"This recent publication adds one more tool to the arsenal researchers
have to discover the molecular structure of proteins," said 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 said. "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 the annual banquet of TTU's Society of Sigma
Xi chapter. Other awards included honoring David Yarbrough for his 20
years of service as secretary/treasurer. Philip Redding, received the
Sigma Xi Regional Science Fair Award.
Four graduate students were inducted as associate members: Duane Hatch, Richard
Mayes, David Sullivan and Girija Shinde. Two faculty members, Motoya Mochida
and Hong Zhang, were inducted as full members.
Sigma Xi Distinguished International Lecturer Leonard Evans, a former
General Motors Corp. scientist, have the keynote address on "A Crash
Course in Traffic Safety." Evans received his doctorate in physics
from Oxford University, is the author of "Traffic Safety and the
Driver," and has published more than 135 articles in professional
journals.-
--Karen Lykins
This information posted 9 MAY 2003
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