Title of project

Synthesis of Norbornene Containing Substrate for Protein Farnesyltransferase

Faculty Advisor

Dr. James Wollack

Department

Chemistry Department

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Synthesis of Norbornene Containing Substrate for Protein Farnesyltransferase

The protein ras is an important part of signaling cells to proliferate and differentiate however, it has also been linked to a few types of human cancers. Such cancers occur when ras has been activated for normal activity but it does not naturally deactivate. Ras is activated through the post-translational modification by protein farnesyltransferase. Protein farnesyltransferase activates ras via prenylation with the tri-isoprenoid called farnesyl diphosphate. It was from the farnesyl diphosphate compound that a non-natural substrate was modeled. The mimicking substrate contained a single isoprenoid group with norbornene attached. This non-natural substrate was synthesized with the potential to be prenylated onto ras via protein farnesyltransferase.