July 11, 2008
Mary Carroll, a graduate student at the UNC Eshelman School of Pharmacy, has received two fellowships for the 2008-09 academic year.
The American Chemical Society Division of Medicinal Chemistry Fellowship selection committee named Carroll its Pfizer Fellow. The fellowship, a nationally competitive award, provides a one-year stipend of $24,000. Carroll will be invited to give a presentation on her research at the fall 2009 national meeting in Washington, D.C., as part of a symposium honoring her and the other fellows. She will receive a plaque and $1,000 to help cover travel and meeting expenses.
Carroll also has been awarded a $6,000 Pre-Doctoral Fellowship from the American Foundation for Pharmaceutical Education. She is eligible for up to two renewals of the fellowship. Because of AFPE policy regarding external awards, Carroll will be able to accept only the funds from the Pfizer Fellowship for the 2008-09 academic year, but she will be eligible to apply for renewal of the AFPE award the following year.
Carroll, who is in the lab of Associate Professor Andrew Lee, PhD, in the Division of Medicinal Chemistry and Natural Products, joined the school in 2006 after earning a BS with honors in biochemistry from Elizabethtown College in Pennsylvania. Her research uses high-field, multi-dimensional NMR spectroscopy to characterize the dynamics of the enzyme dihydrofolate reductase (DHFR).
DHFR reduces dihydrofolate to tetrahydrofolate, a form of folic acid essential to rapidly dividing cells. Because of its function, DHFR is an important drug target for treating diseases that are characterized by rapid cell proliferation, such as cancer, bacterial infections, and malaria.
Carroll says that DHFR, from a biophysical standpoint, is also a model enzyme for studying dynamics. Her project, being completed in collaboration with Associate Professor Scott Singleton’s lab, aims to identify regions of the protein that dynamically assist in the ejection of DHFR inhibitors.
“More generally speaking, this project could provide information on how to develop better inhibitors of DHFR that are not released as rapidly as those already used clinically,” Carroll says. “Further, this same approach could be applied to other pharmaceutically relevant proteins to understand drug release in other systems.”
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