Protein farnesyltransferase (PFTase) has been attributed to the cell division cascade, making it an interesting target of study for cancer research. PFTase site-specifically transfers isoprenoid-containing groups to proteins ending in the specific amino acid sequence CVIA via farnesylation. This farnesylation process can be studied through the synthesis of non-natural substrates that can be modified post-prenylation to express characteristics of interest such as fluorescence. Here an alkyne-containing isoprenid mimic is reported that can be enzymatically phosphorylated and incorporated into CVIA proteins. This mimic contains one more carbon than previously reported alkyne substrates. This will allow for future study on the role that isoprenoid length has on prenyl transferase activity.

Synthesis of an alkyne-containing isoprenoid mimic for the investigation of the role of substrate length on prenyl transferase activity

249th National Meeting (2015)

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