CHED 222 |
| RAS proteins function as a molecular switch for cell growth. Considerable attention has been directed toward the RAS signaling pathway since 30% of all human cancers contain mutant RAS proteins. One method to target RAS oncogenes is the design of farnesyl pyrophosphate mimetics that serve as competitive inhibitors of the enzyme farnesyl protein transferase (FPTase). Farnesyl pyrophosphate is composed of two structural units, a hydrophobic farnesyl “tail” and a polar diphosphate “head.” While drug companies have focused primarily on the design of novel ‘head” mimetics of farnesyl pyrophosphate, our research focuses on modification of the farnesyl “tail”. Through an eight step synthetic sequence, “tails” are currently being prepared that incorporate two aromatic rings. It is anticipated that these farnesyl analogues will bind tighter to the FPTase active site due to intermolecular interactions between the “tail” and the aromatic amino acid residues that have been shown to line the enzyme pocket. |
|
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 |