ORGN 470 |
| Erin E. Pusateri1, Andrew D. Hamilton1, Dora Carrico1, Said M. Sebti2, Michael H. Gelb3, Wesley C Van Voorhis4, and Oliver Hucke5. (1) Department of Chemistry, Yale University, 225 Prospect St., P.O. Box 208107, New Haven, CT 06520-8107, (2) Department of Biochemistry and Molecular Biology, University of South Florida, H. Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612, (3) Department of Chemistry, University of Washington, Seattle, WA 98195, (4) Infectious Diseases, University of Washington, 1959 Pacific Ave. NE, Seattle, WA 98195-1700, (5) Department of Biochemistry, University of Washington, Seattle, WA 98195 |
| In recent years, protein farnesyltransferase has been a major target in the search for novel anticancer agents. We have successfully developed peptidomimetics that exhibit subnanomolar inhibition of mammalian farnesyltransferase activity. The design of these inhibitors was based on the CaaX tetrapeptide; the key sequence recognized by farnesyltransferase. Recently, we have shown that farnesyltransferase from the malaria parasite, P. falciparum can be inhibited in a similar manner. By structurally modifying our current CaaX peptidomimetics, we are investigating the potential application of our inhibitors as antimalarial agents. Details of the synthesis and inhibitory activity of these novel antimalarial peptidomimetics will be presented. |
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Total Synthesis, Process R&D, Combinatorial, Bioorganic, Physical Organic Chemistry
8:00 PM-10:00 PM, Tuesday, August 24, 2004 Pennsylvania Convention Center -- Hall D, Poster
Sci-Mix
Division of Organic Chemistry |