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Journal of Undergraduate Chemistry Research

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Mutant RAS proteins are associated with 30% of all human cancers. Unregulated cell growth caused by mutant RAS proteins can be prevented by RAS farnesyl protein transferase (FPTase) inhibitors. A novel FPTase inhibitor has been synthesized incorporating a modified farnesyl “tail” and a customized diphosphate “head”. It is anticipated that the modified “tail”, incorporating a phenyl substituent, will bind more tightly to FPTase due to nonbonding interactions between the aromatic ring and ten aromatic amino acid residues that line the enzyme active site. The altered polar “head”, designed from L-aspartic acid, has already been shown to mimic the natural substrate’s diphosphate moiety. It is anticipated that the bioactivity of the novel compound presented in this research will illustrate the relevance of modifications to the farnesyl “tail” in the design of farnesyl diphosphate mimetics.


The article originally appeared in the spring 2022 issue of the Journal of Undergraduate Chemistry Research:



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