Stephanie E. Sen

Associate Professor Organic and Bioorganic Chemistry B.A., Bryn Mawr College, 1984 Ph.D., State University of New York Stony Brook, 1989 Dround Foundation Fellow, Research Institute of Scripps Clinic, 1989-90 NIH Postdoctoral Fellow, Research Institute of Scripps Clinic, 1990 NIH Postdoctoral Fellow, Stanford University, 1990-91 Phone: (317)274-6889 Email: sen@chem.iupui.edu Research Publications Sen Lab Homepage

Research

Our work currently relates to three areas: i) juvenile hormone (JH) metabolism; ii) biomimetic polyene cyclizations; and iii) the development of new enzyme mimics. While the specific goals for each project varies, they all ultimately relate to better understanding how enzymes catalyze chemical transformations. To do so, we utilize a combination of organic, biochemical, and computational methods.

Development of Insect Juvenile Hormone Inhibitors
Insects control their growth, morphology, behavior, and sexuality with a complicated array of hormones. We are interested in understanding, at the molecular level, how the insect hormone, JH, is made and then use this information, construct compounds that will selectively inhibit its formation. Three specific enzymes related to JH production are currently under investigation, including prenyltransferase, farnesol dehydrogenase, and isopentenyl diphosphate isomerase. The long range goals of this project is to provide new targets for insecticide development.

Biomimetic Polyene Cyclizations
Bimimicry is the process whereby natural processes are duplicated under artificial conditions. In this regard, we are actively pursuing the development of new methods for steroid and related polycycle production, that mimic naturally-occurring enzymes. Zeolites, or molecular sieves, are both porous and acidic inorganic materials, which we believe can function as surrogates of polyene cyclization enzymes, such as oxidosqualene cyclase. Development of this type of cyclization methodology could greatly expand the chemistÕs synthetic repertoire by allowing the preparation of both naturally occurring and unnatural compounds.

Antibody-Assisted Chemical Transformations
Antibodies, prepared from the immune systems of higher organisms, are highly efficient receptors. While their overall structures are quite similar, antibodies contain a binding region which has been fine tuned for a specific antigen. This characteristic can be used to prepare proteins that serve as either chiral templates for regio- and/or enantioselective chemical reactions or as catalysts. The latter "abzymes" have the potential of performing transformations, which are thus far inaccessible using chemical or enzymatic methods. We are currently utilizing antibody technology to develop novel detoxifying agents.

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Recent Publications

S. E. Sen, D. C. Brown, A. E. Sperry and J. R. Hitchcock "Prenyltransferase of larval and adult M. sexta corpora allata" Insect Biochemistry & Molecular Biology 2007, 37, 29-40.

M. Cusson, C. Beliveau, S. E. Sen, S. Vandermoten, R. G. Rutledge, D. Stewart, F. Francis, E. Haubruge, P. Rehse, D. J. Huggins, A. P. G. Dowling and G. H. Grant "Characterization and tissue-specific expression of two lepidopteran farnesyl diphosphate synthase homologs: Implications for the biosynthesis of ethyl-substituted juvenile hormones" Proteins: Structure, Function & Bioinformatics 2006, 65, 742-758.

S. E. Sen, J. R. Hitchcock, J. L. Jordan and T. Richard "Juvenile hormone biosynthesis in M. sexta: Substrate specificity of insect prenyltransferase utilizing homologous diphosphate analogs" Insect Biochemistry & Molecular Biology 2006, 36, 827-834.

S. E. Sen, A. E. Sperry, M. Childress and D. E. Hannemann "Juvenile hormone biosynthesis in moths: Synthesis and evaluation of farnesol homologs as alternate substrates of farnesol oxidase" Insect Biochemistry & Molecular Biology 2003, 33, 601-607.

S. E. Sen and A. E. Sperry "Partial purification of a farnesyl diphosphate synthase from whole-body Manduca sexta" Insect Biochemistry & Molecular Biology 2002, 32, 889-899.

A. E. Sperry and S. E. Sen "Farnesol oxidation in insects: Evidence that the biosynthesis of insect juvenile hormone is mediated by a specific alcohol oxidase" Insect Biochemistry & Molecular Biology 2001, 31, 171-178.

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