Emily ScottDepartment of Medicinal Chemistry, University of Kansas, Lawrence, KS, USA F1000 Faculty Member (since 21 November 2011)
BIOGRAPHYCURRENT ACADEMIC APPOINTMENTS:
Associate Professor, Department of Medicinal Chemistry, University of Kansas
Courtesy Faculty, Department of Chemistry, University of Kansas
Affiliate Faculty, Department of Molecular Biosciences, University of Kansas
BS, Marine Biology, Texas A&M University at Galveston
PhD, Biochemistry and Cell Biology, Rice University
Postdoc, Biochemistry and Cell Biology, Rice University
Postdoc, Pharmacology and Toxicology, University of Texas Medical Branch
Early Career Achievement Award, Drug Metabolism Division of The American Society for Pharmacology and Experimental Therapeutics
James R Gillette Drug Metabolism Best Paper of 2009 in Drug Metabolism and Disposition
Postdoctoral Scientist Award, Drug Metabolism Division, American Society for Pharmacology and Experimental Therapeutics
NIH National Research Service Award Individual Postdoctoral Fellowship
American Chemical Society
American Society for Pharmacology and Experimental Therapeutics
American Society for Biochemistry and Molecular Biology
The long-term goals of the Scott research program are to understand how the structure and function of cytochrome P450 (CYP) enzymes are related and to exploit this knowledge to benefit human health and disease treatment. Investigations target cytochrome P450 enzymes involved in drug metabolism and procarcinogen activation, as well as those required in physiologically-important endogenous pathways.
One area of emphasis includes the CYP2A and CYP2E subfamilies of these enzymes. CYP2A13 and CYP2A6 are 94% identical, but have differing abilities to activate tobacco-derived nitrosaminoketone procarcinogens. High throughput-screening and identification of differences in the active site architectures of these enzymes have led to the development of selective inhibitors of CYP2A13 in the human respiratory tract. These inhibitors can potentially be used to prevent nitrosamine-associated DNA damage that initiates lung cancer in smokers. Comparisons of the CYP2A enzymes with CYP2E1 are additionally revealing structural features that lead to both functional similarities and differences between cytochrome P450 subfamilies.
A second area of emphasis is human steroidogenesis. Initial structures of the androgen-generating cytochrome P450 17A1 are providing insights into the binding of inhibitors and substrates. Convergent structural, synthetic chemistry, and functional approaches we are probing the reaction mechanisms for the hydroxylase versus lyase capabilities of this multifunctional enzyme and designing inhibitors for the treatment of metastatic prostate cancer.
Technical approaches used in these pursuits include the expression, purification, and stabilization of membrane cytochrome P450 enzymes; steady-state kinetics of ligand binding, catalysis, and inhibition; site-directed mutagenesis; X-ray crystallography; solution NMR; drug design and evaluation; synthetic organic chemistry; and computational methodologies.
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