Bioorganic and Medicinal Chemistry Letters p. 1345 - 1348 (1997)
Update date:2022-08-02
Topics:
Dinsmore, Christopher J.
Williams, Theresa M.
Hamilton, Kelly
O'Neill, Timothy J.
Rands, Elaine
Koblan, Kenneth S.
Kohl, Nancy E.
Gibbs, Jackson B.
Graham, Samuel L.
Hartman, George D.
Oliff, Allen I.
The design and synthesis of simple nonpeptide inhibitors of farnesyl-protein transferase (FTase) are described. Cysteine-derived diarylether frameworks are appropriate structural replacements for the C-terminal tetrapeptide portion of the Ras protein, and possess in vitro potency against FTase. Inhibitory activity is dependent on the ring-substitution pattern, and does not require the presence of a C-terminal carboxylate group.
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