CHED 221 |
| RAS proteins play an essential role in the signal transduction pathways which regulate cell proliferation. Single point mutations in RAS are associated with approximately 30% of all human cancers. The addition of a fifteen carbon terpene chain to the RAS protein, catalyzed by the enzyme farnesyl protein transferase (FPTase), has been shown to be the key step in allowing RAS proteins to regulate cell growth. Compounds that inhibit this enzyme are potential chemotherapeutic agents. Farnesyl pyrophosphate and RAS proteins are the two natural substrates for FPTase. Current work is focused on the design and synthesis of novel farnesyl pyrophosphate mimetics that will serve as competitive FPTase inhibitors. The specific targets in this project are analogues that will incorporate one aromatic ring in the farnesyl “tail”. It is anticipated that these compounds will illustrate the importance of nonbonding interactions in enzymatic recognition of the farnesyl chain. |
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Undergraduate Research Poster Session: Organic Chemistry
2:00 PM-4:00 PM, Monday, 29 August 2005 Washington DC Convention Center -- Hall A, Poster
Division of Chemical Education |